organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)


enzyme_display_name: UMP kinase

organism: Bacillus subtilis (strain 168)

substrate_name: ATP

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: cofactor ATP

proof_lines: In the absence of GTP, the activity is less than 10% of its maximum activity. Is unstable in the absence of UTP. Positive cooperativity is observed with ATP as variable substrate, but it is strongly reduced in the presence of GTP. GTP enhan

enzyme: UMP kinase

substrate: ATP

source: uniprot


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: Unknown

km_display: Not reported

proof_lines: Positive cooperativity is observed with ATP as variable substrate, but it is strongly reduced in the presence of GTP. GTP enhances the affinity for ATP.

substrate: Unknown


organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

substrate_name: UMP (in the absence of GTP)

proof_lines: Positive cooperativity is observed with ATP as variable substrate, but it is strongly reduced in the presence of GTP. GTP enhances the affinity for ATP whereas UTP decreases it.

substrate: UMP (in the absence of GTP)


organism: Ureaplasma parvum serovar 3 (strain ATCC 700970)

substrate_name: UMP

proof_lines: Positive cooperativity is observed with ATP as variable substrate, but it is abolished in the presence of UTP.

substrate: UMP


organism: Arabidopsis thaliana

verification_status: unverified

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

data_origin: experimental

status: unverified


organism: Escherichia coli (strain K12)

substrate_name: ATP (in the presence of 0.3 mM UMP)

substrate: ATP (in the presence of 0.3 mM UMP)


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate_name: ATP (in the absence of GTP)

substrate: ATP (in the absence of GTP)


organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: UMP (at pH 7.2)

assay_conditions_summary: pH 7.2; cofactor ATP

substrate: UMP (at pH 7.2)


enzyme_display_name: holo-[acyl-carrier-protein] synthase

organism: Homo sapiens

substrate_name: magnesium

assay_conditions_summary: cofactor CoA

enzyme: holo-[acyl-carrier-protein] synthase

substrate: magnesium


enzyme_display_name: indole-3-glycerol-phosphate synthase

organism: Bacillus subtilis

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_source: UniProtKB reviewed accession P03964 direct lookup on 2026-06-05

enzyme: indole-3-glycerol-phosphate synthase


organism: Escherichia coli

sequence_source: UniProtKB reviewed accession P00909 direct lookup on 2026-06-05; row-specific truncation reconstructed from residues 1-259

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) wildtype truncated TrpC (aa 1-259)


source_db: oed

kcat_over_km_origin: calculated

sequence_source: UniProtKB reviewed accession P00909 direct lookup on 2026-06-05

source: oed


sequence_source: UniProtKB reviewed accession P00909 direct lookup on 2026-06-05; variant sequence not reconstructed

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) mutant K55S


proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) mutant IGPS[1:252FAG]

proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) mutant IGPS[1-259]


organism: Mycobacterium tuberculosis

source_db: brenda

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 direct lookup on 2026-06-05; N189A reconstructed from canonical sequence and applied mutation signature N189A to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 direct lookup on 2026-06-05; H170A reconstructed from canonical sequence and applied mutation signature H170A to reconstruct the assayed variant sequence.


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 FASTA direct check; reconstructed D61C variant from canonical sequence and applied mutation signature D61C to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555

proof_lines: pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye PyMPO


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 FASTA direct check; reconstructed R18C variant from canonical sequence and applied mutation signature R18C to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye Alexa Fluor 555

proof_lines: pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye PyMPO


sequence_source: UniProtKB Q06121 FASTA direct check; reconstructed D61C variant from canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 FASTA direct check; reconstructed E51Q variant from canonical sequence and applied mutation signature E51Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 FASTA direct check; reconstructed R182A variant from canonical sequence and applied mutation signature R182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 FASTA direct check; reconstructed K53R variant from canonical sequence and applied mutation signature K53R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q06121 FASTA direct check; reconstructed K53R variant from canonical sequence


sequence_source: UniProtKB Q06121 FASTA direct check; reconstructed R182A variant from canonical sequence


sequence_source: UniProt REST direct accession lookup for P9WFX7 on 2026-06-05


source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

proof_lines: increased Km value in the presence of ATB107


organism: Pseudomonas aeruginosa

sequence_source: UniProt REST direct accession lookup for P20577 on 2026-06-05


organism: Pyrococcus furiosus

sequence_source: UniProt REST direct accession lookup for Q8U088 on 2026-06-05


sequence_source: UniProt REST direct accession lookup for Q06121 plus selected BRENDA mutation note on 2026-06-05

mutation_type: deletion

proof_lines: N-terminal deletion mutant lacking 26 amino acids, pH 7.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup for Q06121 plus selected mutation signature on 2026-06-05 and applied mutation signature R18C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA R191A mutation note and applied mutation signature R191A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA V169A mutation note and applied mutation signature V169A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA S64A mutation note and applied mutation signature S64A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA P63A mutation note and applied mutation signature P63A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA L193A mutation note and applied mutation signature L193A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P9WFX7 checked against selected BRENDA N192A mutation note


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA L196A mutation note and applied mutation signature L196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WFX7 plus selected BRENDA E168A mutation note and applied mutation signature E168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05; K53Q reconstructed from the canonical sequence. and applied mutation signature K53Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05; E51Q reconstructed from the canonical sequence. and applied mutation signature E51Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines:
pH 7.5, 75°C, wild-type enzyme
wild-type, pH 7.5, 60°C
wild-type, pH 7.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05; E210Q reconstructed from the canonical sequence. and applied mutation signature E210Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05; E210Q reconstructed from the canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05; M237T reconstructed from the canonical sequence. and applied mutation signature M237T to reconstruct the assayed variant sequence.


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q06121 and applied mutation signature M237T to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-State Kinetic Parameters for Wild-Type ssIGPS and Activated Variants at 25 C (Biochemistry 2018, 57, 3265-3277); printed column heads variant | kcat (s-1) | KM (uM) | kcat/KM (M-1 s-1). Table 1, variant row M237T; column kcat (s-1) = 0.23; column KM (uM) = 2.9; column kcat/KM (M-1 s-1) = 0.08 x 10^6. The value printed after each plus/minus sign on the same line is the printed uncertainty of the cell beside it. captured primary segment: variant M237T | kcat 0.23 s^-1 | KM 2.9 uM | kcat/KM 0.08 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.23 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.23 s^(-1). Km: printed Table 1 cell 2.9 in a column headed KM (uM); 1 uM is 1/1000 mM, so 2.9 / 1000 = 0.0029 mM. kcat/Km: printed Table 1 cell 0.08 x 10^6 in a column headed kcat/KM (M-1 s-1); that literal is 80000 M-1 s-1 and 1 M-1 s-1 is 0.001 s-1 mM-1, so 80000 / 1000 = 80.0 s^(-1)*mM^(-1). The quotient of the same line's own two printed cells is 0.23 / 0.0029 = 79.31034482758622 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row M237T: kcat = 0.23 in a column headed kcat (s-1); KM = 2.9 in a column headed KM (uM); kcat/KM = 0.08 x 10^6 in a column headed kcat/KM (M-1 s-1).

row_label: Table 1, variant row M237T

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q06121 direct REST/FASTA check on 2026-06-05; G212E reconstructed from the canonical sequence. and applied mutation signature G212E to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

sequence_source: UniProtKB:Q56319 canonical sequence plus PMID:16342933 tIGPSDelta(1-25) abstract evidence

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: N-terminal deletion mutant lacking 25 amino acids, pH 7.5, 25°C


sequence_source: UniProtKB:Q56319 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 direct accession check plus row-specific single-substitution reconstruction and applied mutation signature L236Q to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q06121 and applied mutation signature F246S to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-State Kinetic Parameters for Wild-Type ssIGPS and Activated Variants at 25 C (Biochemistry 2018, 57, 3265-3277); printed column heads variant | kcat (s-1) | KM (uM) | kcat/KM (M-1 s-1). Table 1, variant row F246S; column kcat (s-1) = 0.32; column KM (uM) = 1.3; column kcat/KM (M-1 s-1) = 0.24 x 10^6. The value printed after each plus/minus sign on the same line is the printed uncertainty of the cell beside it. captured primary segment: variant F246S | kcat 0.32 s^-1 | KM 1.3 uM | kcat/KM 0.24 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.32 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.32 s^(-1). Km: printed Table 1 cell 1.3 in a column headed KM (uM); 1 uM is 1/1000 mM, so 1.3 / 1000 = 0.0013 mM. kcat/Km: printed Table 1 cell 0.24 x 10^6 in a column headed kcat/KM (M-1 s-1); that literal is 240000 M-1 s-1 and 1 M-1 s-1 is 0.001 s-1 mM-1, so 240000 / 1000 = 240.0 s^(-1)*mM^(-1). The quotient of the same line's own two printed cells is 0.32 / 0.0013 = 246.15384615384616 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row F246S: kcat = 0.32 in a column headed kcat (s-1); KM = 1.3 in a column headed KM (uM); kcat/KM = 0.24 x 10^6 in a column headed kcat/KM (M-1 s-1).

row_label: Table 1, variant row F246S

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q06121 and applied mutation signature L236Q to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-State Kinetic Parameters for Wild-Type ssIGPS and Activated Variants at 25 C (Biochemistry 2018, 57, 3265-3277); printed column heads variant | kcat (s-1) | KM (uM) | kcat/KM (M-1 s-1). Table 1, variant row L236Q; column kcat (s-1) = 0.20; column KM (uM) = 3.4; column kcat/KM (M-1 s-1) = 0.06 x 10^6. The value printed after each plus/minus sign on the same line is the printed uncertainty of the cell beside it. captured primary segment: variant L236Q | kcat 0.20 s^-1 | KM 3.4 uM | kcat/KM 0.06 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.20 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.2 s^(-1). Km: printed Table 1 cell 3.4 in a column headed KM (uM); 1 uM is 1/1000 mM, so 3.4 / 1000 = 0.0034 mM. kcat/Km: printed Table 1 cell 0.06 x 10^6 in a column headed kcat/KM (M-1 s-1); that literal is 60000 M-1 s-1 and 1 M-1 s-1 is 0.001 s-1 mM-1, so 60000 / 1000 = 60.0 s^(-1)*mM^(-1). The quotient of the same line's own two printed cells is 0.2 / 0.0034 = 58.82352941176471 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row L236Q: kcat = 0.20 in a column headed kcat (s-1); KM = 3.4 in a column headed KM (uM); kcat/KM = 0.06 x 10^6 in a column headed kcat/KM (M-1 s-1).

row_label: Table 1, variant row L236Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q06121 and applied mutation signature G212E to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-State Kinetic Parameters for Wild-Type ssIGPS and Activated Variants at 25 C (Biochemistry 2018, 57, 3265-3277); printed column heads variant | kcat (s-1) | KM (uM) | kcat/KM (M-1 s-1). Table 1, variant row G212E; column kcat (s-1) = 0.16; column KM (uM) = 21.7; the column kcat/KM (M-1 s-1) prints an inequality on this line rather than a determined value. The value printed after each plus/minus sign on the same line is the printed uncertainty of the cell beside it. captured primary segment: variant G212E | kcat 0.16 s^-1 | KM 21.7 uM

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.16 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.16 s^(-1). Km: printed Table 1 cell 21.7 in a column headed KM (uM); 1 uM is 1/1000 mM, so 21.7 / 1000 = 0.0217 mM. kcat/Km: the table prints no determined efficiency value on this line, so the efficiency is taken as the exact quotient of the same line's own two printed cells, 0.16 / 0.0217 = 7.373271889400922 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row G212E: kcat = 0.16 in a column headed kcat (s-1); KM = 21.7 in a column headed KM (uM). The efficiency column of this line prints an inequality, not a determined value, so no efficiency cell is read from it.

row_label: Table 1, variant row G212E


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06121 direct accession check plus row-specific single-substitution reconstruction and applied mutation signature F246S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q06121 direct accession check


source_license: CC BY 4.0; CC BY-NC-ND 4.0

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=60°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: brenda skid


organism: Saccharomyces cerevisiae

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of D129A on 2026-06-05 and applied mutation signature D129A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of E181Q on 2026-06-05 and applied mutation signature E181Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q9NRN7 direct JSON/FASTA lookup on 2026-06-05


substrate_name: Acetyl-CoA; Apo-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of K185A on 2026-06-05 and applied mutation signature K185A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site K185A

substrate: Acetyl-CoA; Apo-[acyl-carrier protein]


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of E181A on 2026-06-05 and applied mutation signature E181A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of R86A on 2026-06-05 and applied mutation signature R86A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of Q112E on 2026-06-05 and applied mutation signature Q112E to reconstruct the assayed variant sequence.


substrate_name: Apo-[acyl-carrier protein]; Acetyl-CoA

sequence_source: UniProtKB reviewed accession Q9NRN7 direct lookup plus reviewer reconstruction of E181Q on 2026-06-05

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site E181Q

substrate: Apo-[acyl-carrier protein]; Acetyl-CoA


enzyme_display_name: Indole-3-glycerol phosphate synthase

organism: Sulfolobus solfataricus

table_label: Table 1. Steady-State Kinetic Parameters for Wild-Type ssIGPS and Activated Variants at 25 C (Biochemistry 2018, 57, 3265-3277); printed column heads variant | kcat (s-1) | KM (uM) | kcat/KM (M-1 s-1)

enzyme: Indole-3-glycerol phosphate synthase


sequence_source: UniProt Q06121 checked; selected SABIO-RK note also specifies a C-terminal His6-tag, so the full row-specific tagged construct sequence is unresolved.

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) mutant G212E C-terminal His6-tag


sequence_source: UniProt Q56319 canonical sequence.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_variant_note: Resolved canonical sequence from UniProt Q56319 canonical sequence; D184A reconstructed after confirming canonical residue D at position 184. and applied mutation signature D184A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) mutant D184A


sequence_variant_note: Resolved canonical sequence from UniProt Q56319 canonical sequence; R241A reconstructed after confirming canonical residue R at position 241. and applied mutation signature R241A to reconstruct the assayed variant sequence.


source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0


sequence_source: UniProt Q56319 canonical sequence; D184A reconstructed after confirming canonical residue D at position 184.


sequence_source: UniProt Q56319 canonical sequence; R241A reconstructed after confirming canonical residue R at position 241.

proof_lines: SABIO-RK modifier species: indole-3-glycerol-phosphate synthase(Enzyme) mutant R241A


sequence_source: UniProtKB Q06121 FASTA/REST direct accession lookup retrieved 2026-06-05


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q06121 and applied mutation signature M237T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9NRN7 with mutation reconstruction and applied mutation signature Q112E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9NRN7 with mutation reconstruction and applied mutation signature R47A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9NRN7 with mutation reconstruction and applied mutation signature K185A to reconstruct the assayed variant sequence.


proof_lines:
wild-type
+/-0.04 mM, wild-type
+/-0.003 mM, wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9NRN7 with mutation reconstruction and applied mutation signature E181Q/Q112E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9NRN7 with mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9NRN7 with mutation reconstruction and applied mutation signature R86A to reconstruct the assayed variant sequence.


organism: Bacillus subtilis (strain 168)

substrate_name: coenzyme A

sequence_source: source_record; UniProt P39135 direct check

proof_lines: kcat is 104 min(-1) with a peptide fragment encompassing residues 960-1084 of surfactin synthetase SrfAB subunit as substrate. kcat is 56 min(-1) with a peptide fragment encompassing residues 2006-2123 of surfactin synthetase SrfAB subunit

substrate: coenzyme A


organism: Streptomyces mobaraensis

substrate_name: Streptomyces mobaraensis apo-PCP BlmI

sequence_source: source_record; UniProt Q9F0Q6 direct check

proof_lines: kcat is 11 min(-1) with S.mobaraensis apo-PCP BlmI as substrate and 86 min(-1) with S.glaucescens apo-ACP TcmM as substrate.

substrate: Streptomyces mobaraensis apo-PCP BlmI


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction and applied mutation signature E181Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction and applied mutation signature D129A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction and applied mutation signature H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction and applied mutation signature Q112E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site Q112E


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction and applied mutation signature E181Q/Q112E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site E181Q, Q112E


sequence_source: UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical FASTA with row-specific mutation reconstruction and applied mutation signature K185A to reconstruct the assayed variant sequence.


enzyme_display_name: phosphate acetyltransferase

substrate_name: acetyl-CoA

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

enzyme: phosphate acetyltransferase

substrate: acetyl-CoA


organism: Chlorogonium elongatum

substrate_name: CoA

substrate: CoA


organism: Clostridium kluyveri


organism: Desulfomicrobium sp.

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


organism: Desulfovibrio piger


sequence_source: UniProtKB reviewed accession P77218 (EUTD_ECOLI), explicitly referenced to PMID 21046341 / DOI 10.1007/s12275-010-0091-0

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA


organism: Methanosarcina thermophila

substrate_name: desulfo-CoA

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

substrate: desulfo-CoA


substrate_name: phosphate

assay_conditions_summary: pH 7.2; 298.15 K; cofactor CoA

proof_lines: 25°C, pH 7.2, with respect to acetyl phosphate

substrate: phosphate


enzyme_display_name: catalase

organism: Thermus thermophilus

enzyme: catalase


organism: Ureibacillus thermosphaericus

sequence_source: UniProtKB A0A2H4YCD5; EMBL KY776555/AUD75679.1; PMID 28501604; strain FZSF03

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Vibrio vulnificus

protein_accession_database: NCBI Protein

sequence_source: NCBI Protein KTL38510.1; PMID 28892106; CAT-Vv from Vibrio vulnificus ATCC 43382

smiles: OO


organism: Vigna mungo


organism: Xanthomonas campestris


organism: Zavarzinia compransoris


enzyme_display_name: tyrosine transaminase

organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q9LVY1 direct REST check on 2026-06-05

enzyme: tyrosine transaminase


substrate_name: oxaloacetate

smiles: O=C(O)CC(=O)C(=O)O

substrate: oxaloacetate


smiles: CSCCC(=O)C(=O)O


sequence_source: UniProtKB reviewed accession Q9FN30 direct REST check on 2026-06-05

proof_lines: isoform TAT2, with L-glutamate as cosubstrate, at pH 8.5 and 30°C

proof_lines: isoform TAT2, with L-tyrosine as cosubstrate, at pH 8.5 and 30°C

proof_lines: isoform TAT2, with 2-oxoglutarate as cosubstrate, at pH 8.5 and 30°C


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: phenylpyruvate

substrate: phenylpyruvate


smiles: O=C(O)CCC(=O)C(=O)O


organism: Anchusa officinalis

substrate_name: L-tyrosine

proof_lines:
pH 9.2, 40°C, isoenzyme TAT-3
pH 9.2, 40°C, isoenzyme TAT-1
pH 9.2, 40°C, isoenzyme TAT-2

substrate: L-tyrosine


organism: Rattus norvegicus

proof_lines:
pH 7.6, 37°C, enzyme form III
pH 7.6, 37°C, enzyme form I
pH 7.6, 37°C, enzyme form II


sequence_source: UniProtKB P04694 direct REST/FASTA lookup

assay_conditions_summary: pH 7.5; 310.15 K; buffer 1-mL reaction mixtures containing 150 mM triethanolamine

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Wild type enzyme column. In the Km (mM) block the substrate-pair row p-hydroxyphenylpyr reads 1.2; in the kcat (sec-1) block the same substrate-pair row reads 165; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 138, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.2 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.2 mM. kcat: printed Table 2 cell 165 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 165 s^(-1). kcat/Km: printed Table 2 cell 138 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 138 x 10^3 M-1 s-1 = 138000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 138000.0 / 1000 = 138.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Wild type enzyme column, substrate-pair row p-hydroxyphenylpyr: Km = 1.2 mM; kcat = 165 sec-1; printed kcat/Km = 138 x 10^3 M-1 s-1.

row_label: Table 2, Wild type column, substrate-pair row p-hydroxyphenylpyr

table_label: Table 2: Kinetic parameters for the overall reactions of the N-truncated recombinant rat TAT, Arg315Lys, and Asn54Ser variants (Protein Science 2003, 12:1039-1050)


substrate_name: 2-Oxoglutarate; L-Tyrosine

sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 canonical sequence plus PMID 12717026 R315K mutation label and applied mutation signature R315K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine transaminase(Enzyme) mutant R315K

substrate: 2-Oxoglutarate; L-Tyrosine


substrate_name: L-Glutamate

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Wild type enzyme column. In the Km (mM) block the substrate-pair row L-Glutamate reads 2.2; in the kcat (sec-1) block the same substrate-pair row reads 210; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 96, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.2 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.2 mM. kcat: printed Table 2 cell 210 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 210 s^(-1). kcat/Km: printed Table 2 cell 96 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 96 x 10^3 M-1 s-1 = 96000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 96000.0 / 1000 = 96.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Wild type enzyme column, substrate-pair row L-Glutamate: Km = 2.2 mM; kcat = 210 sec-1; printed kcat/Km = 96 x 10^3 M-1 s-1.

row_label: Table 2, Wild type column, substrate-pair row L-Glutamate

substrate: L-Glutamate


substrate_name: L-Tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04694 and applied mutation signature R315K to reconstruct the assayed variant sequence.

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Arg315Lys enzyme column. In the Km (mM) block the substrate-pair row L-Tyrosine reads 2.3; in the kcat (sec-1) block the same substrate-pair row reads 510; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 222, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.3 mM. kcat: printed Table 2 cell 510 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 510 s^(-1). kcat/Km: printed Table 2 cell 222 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 222 x 10^3 M-1 s-1 = 222000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 222000.0 / 1000 = 222.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Arg315Lys enzyme column, substrate-pair row L-Tyrosine: Km = 2.3 mM; kcat = 510 sec-1; printed kcat/Km = 222 x 10^3 M-1 s-1.

row_label: Table 2, Arg315Lys column, substrate-pair row L-Tyrosine

substrate: L-Tyrosine


substrate_name: L-Tyrosine; 2-Oxoglutarate

substrate: L-Tyrosine; 2-Oxoglutarate


column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Wild type enzyme column. In the Km (mM) block the substrate-pair row 2-oxoglutarate reads 0.40; in the kcat (sec-1) block the same substrate-pair row reads 566; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 1415, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.40 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.40 mM. kcat: printed Table 2 cell 566 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 566 s^(-1). kcat/Km: printed Table 2 cell 1415 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 1415 x 10^3 M-1 s-1 = 1415000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 1415000.0 / 1000 = 1415.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Wild type enzyme column, substrate-pair row 2-oxoglutarate: Km = 0.40 mM; kcat = 566 sec-1; printed kcat/Km = 1415 x 10^3 M-1 s-1.

row_label: Table 2, Wild type column, substrate-pair row 2-oxoglutarate


sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 canonical sequence plus PMID 12717026 N54S mutation label and applied mutation signature N54S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine transaminase(Enzyme) mutant N54S


column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Arg315Lys enzyme column. In the Km (mM) block the substrate-pair row L-Glutamate reads 1.9; in the kcat (sec-1) block the same substrate-pair row reads 199; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 105, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.9 mM. kcat: printed Table 2 cell 199 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 199 s^(-1). kcat/Km: printed Table 2 cell 105 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 105 x 10^3 M-1 s-1 = 105000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 105000.0 / 1000 = 105.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Arg315Lys enzyme column, substrate-pair row L-Glutamate: Km = 1.9 mM; kcat = 199 sec-1; printed kcat/Km = 105 x 10^3 M-1 s-1.

row_label: Table 2, Arg315Lys column, substrate-pair row L-Glutamate


organism: Trypanosoma cruzi

substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P33447 direct REST/FASTA lookup; N17S reconstructed from the canonical sequence and applied mutation signature N17S to reconstruct the assayed variant sequence.

substrate: L-alanine


sequence_source: UniProtKB reviewed P33447 direct REST/FASTA lookup


organism: Variovorax paradoxus

substrate_name: (S)-beta-phenylalanine

proof_lines: enzyme shows substrate inhibition, pH 7.6, 30°C

substrate: (S)-beta-phenylalanine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


proof_lines: isoform TAT1, with L-glutamate as cosubstrate, at pH 8.5 and 30 C

proof_lines: isoform TAT1, with L-tyrosine as cosubstrate, at pH 8.5 and 30 C

proof_lines: isoform TAT1, with 2-oxoglutarate as cosubstrate, at pH 8.5 and 30 C


organism: Klebsiella pneumoniae

substrate_name: 4-Methylthio-2-oxobutanoate; L-Tyrosine

substrate: 4-Methylthio-2-oxobutanoate; L-Tyrosine


organism: Leishmania donovani

proof_lines: N-terminal domain, with pyruvate as cosubstrate, at pH 8.0 and 37 C

proof_lines: C-terminal domain, with pyruvate as cosubstrate, at pH 8.0 and 37 C


organism: Petunia x hybrida


substrate_name: L-phenylalanine

proof_lines: cosubstrate 4-hydroxyphenylpyruvate, pH 10.0, 30 C

proof_lines: cosubstrate phenylalanine, pH 10.0, 30 C

substrate: L-phenylalanine


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: Phenylpyruvate aminotransferase

enzyme_name_source: UniProtKB direct accession lookup

sequence_source: UniProtKB V5M241 REST/FASTA direct lookup on 2026-06-05

enzyme: Phenylpyruvate aminotransferase


enzyme_display_name: Tyrosine aminotransferase

sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 REST/FASTA direct lookup on 2026-06-05 and applied mutation signature N54S to reconstruct the assayed variant sequence.

enzyme: Tyrosine aminotransferase


sequence_source: UniProtKB P04694 REST/FASTA direct lookup on 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 REST/FASTA direct lookup on 2026-06-05 and applied mutation signature R315K to reconstruct the assayed variant sequence.


substrate_name: tryptophan (at pH 7.4 and 10 mM KMTB)

substrate: tryptophan (at pH 7.4 and 10 mM KMTB)


organism: Mus musculus

substrate_name: tyrosine

substrate: tyrosine


sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


organism: Tapinella panuoides


enzyme_display_name: pantothenate kinase

organism: Homo sapiens

substrate_name: (R)-pantothenate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: recombinant isozyme mPanK2, pH 7.5, 37°C

proof_lines: recombinant isozyme iPanK2, pH 7.5, 37°C

enzyme: pantothenate kinase

substrate: (R)-pantothenate


organism: Thermotoga maritima

substrate_name: (R)-Pantothenate

sequence_source: UniProtKB reviewed Swiss-Prot accession Q9WZY5

substrate: (R)-Pantothenate


substrate_name: (R)-Pantothenate; ATP

substrate: (R)-Pantothenate; ATP


organism: Staphylococcus aureus

sequence_source: UniProtKB reviewed accession Q2FWC7, fetched 2026-06-05

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: ATP; (R)-Pantothenate

substrate: ATP; (R)-Pantothenate


substrate_name: ATP

substrate: ATP


substrate_name: N-Pentylpantothenamide

substrate: N-Pentylpantothenamide


substrate_name: N-Heptylpantothenamide

substrate: N-Heptylpantothenamide


organism: Thermococcus kodakaraensis

assay_conditions_summary: pH 8; 315.15 K; cofactor ATP


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot accession P0A6I3 with row-specific F247V reconstruction and applied mutation signature F247V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant F247V


source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed Swiss-Prot accession P0A6I3

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: at pH 7.6, temperature not specified in the publication

proof_lines: pH 7.5, 37°C, recombinant His-tagged enzyme

source_databases_merged: sabio_rk brenda skid


assay_conditions_summary: pH 6; 293.00 K; cofactor ATP


organism: Helicobacter pylori

sequence_source: UniProtKB reviewed Swiss-Prot accession O25533

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


sequence_source: UniProtKB reviewed Swiss-Prot accession Q9BZ23


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_source: UniProtKB:Q9H999 / PANK3_HUMAN direct accession lookup on 2026-06-05; reviewed Homo sapiens pantothenate kinase 3 annotated with EC 2.7.1.33.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H999 canonical sequence with row-specific R207W substitution computed on 2026-06-05 from selected mutation_signature R207W. and applied mutation signature R207W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant R207W His-tagged


proof_lines:
isoform PanK3, at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.5


sequence_source: UniProtKB:Q8R2W9 / PANK3_MOUSE direct accession lookup on 2026-06-05; reviewed Mus musculus pantothenate kinase 3 annotated with EC 2.7.1.33.


sequence_source: UniProtKB:Q8K4K6-2 isoform sequence lookup on 2026-06-05; Q8K4K6 is reviewed Mus musculus pantothenate kinase 1, and isoform 2 is named PanK1-beta.


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WPA7 / COAA_MYCTU direct accession lookup on 2026-06-05; reviewed Mycobacterium tuberculosis strain H37Rv pantothenate kinase annotated with EC 2.7.1.33.

proof_lines: 25°C, pH 7.8, determined from coupled assay

proof_lines: 25°C, pH 7.8, determined by isothermal titration calorimetry


organism: Picrophilus oshimae

substrate_name: pantothenate

sequence_source: UniProtKB:Q6L2I5 / Q6L2I5_PICTO direct accession lookup on 2026-06-05; unreviewed Picrophilus torridus strain entry under Picrophilus oshimae taxonomy, annotated as pantothenate kinase EC 2.7.1.33.

substrate: pantothenate


substrate_name: L-Tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04694 and applied mutation signature N54S to reconstruct the assayed variant sequence.

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Asn54Ser enzyme column. In the Km (mM) block the substrate-pair row L-Tyrosine reads 5.3; in the kcat (sec-1) block the same substrate-pair row reads 132; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 25, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 5.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 5.3 mM. kcat: printed Table 2 cell 132 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 132 s^(-1). kcat/Km: printed Table 2 cell 25 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 25 x 10^3 M-1 s-1 = 25000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 25000.0 / 1000 = 25.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Asn54Ser enzyme column, substrate-pair row L-Tyrosine: Km = 5.3 mM; kcat = 132 sec-1; printed kcat/Km = 25 x 10^3 M-1 s-1.

row_label: Table 2, Asn54Ser column, substrate-pair row L-Tyrosine

substrate: L-Tyrosine


substrate_name: L-tyrosine

sequence_source: UniProtKB REST direct accession check: P04694

substrate: L-tyrosine


column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Asn54Ser enzyme column. In the Km (mM) block the substrate-pair row p-hydroxyphenylpyr reads 1.3; in the kcat (sec-1) block the same substrate-pair row reads 5.9; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 4.5, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.3 mM. kcat: printed Table 2 cell 5.9 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 5.9 s^(-1). kcat/Km: printed Table 2 cell 4.5 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 4.5 x 10^3 M-1 s-1 = 4500.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 4500.0 / 1000 = 4.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Asn54Ser enzyme column, substrate-pair row p-hydroxyphenylpyr: Km = 1.3 mM; kcat = 5.9 sec-1; printed kcat/Km = 4.5 x 10^3 M-1 s-1.

row_label: Table 2, Asn54Ser column, substrate-pair row p-hydroxyphenylpyr


organism: Thermococcus litoralis

substrate_name: 2-Oxoglutarate; L-Tyrosine

substrate: 2-Oxoglutarate; L-Tyrosine


substrate_name: pyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check: P33447; variant reconstructed from selected mutation_signature R20A and applied mutation signature R20A to reconstruct the assayed variant sequence.

substrate: pyruvate


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: recombinant isozyme PanK1beta, pH 7.0, 37°C


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q8L5Y9 canonical sequence from direct accession lookup


organism: Aspergillus nidulans

sequence_source: UniProtKB:O93921 canonical sequence from direct accession lookup


organism: Bacillus subtilis

sequence_source: UniProtKB:P37564 canonical sequence from direct accession lookup


organism: Entamoeba histolytica

sequence_source: UniProtKB:B1N2P3 canonical sequence from direct accession lookup

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I3 canonical sequence with row-specific H177Q substitution reconstructed during review and applied mutation signature H177Q to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant H177Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I3 canonical sequence with row-specific R106A substitution reconstructed during review and applied mutation signature R106A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant R106A


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: pantothenate (at 50 degrees Celsius)

substrate: pantothenate (at 50 degrees Celsius)


substrate_name: indole-3-pyruvic acid (at pH 8.5 and 37 degrees Celsius)

proof_lines: kcat is 2.5 min(-1) with indole-3-pyruvic acid as substrate. kcat is 1.9 min(-1) with L-Met as substrate. kcat is 3.16 min(-1) with L-Phe as substrate (at pH 8.5 and 37 degrees Celsius).


organism: Caenorhabditis elegans

substrate_name: tyrosine (para-tyrosine)

proof_lines: kcat is 2852 sec(-1) with tyrosine (para-tyrosine) as substrate (PubMed:31043480). kcat is 2520 sec(-1) with meta-tyrosine as substrate (PubMed:31043480).

substrate: tyrosine (para-tyrosine)


substrate_name: p-nitrophenylphosphate

proof_lines: kcat is 1.99 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.26 sec(-1) with phosphopantetheine as substrate. kcat is 0.94 sec(-1) with 4'-phosphopantotheine-S-sulfonate as substrate. kcat is 0.52 sec(-1) with 4'-phosphopantothe

substrate: p-nitrophenylphosphate


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: pantothenate (in the absence of ammonium)

proof_lines: kcat is 12.5 min(-1) for the phosphorylation of pantothenate in the absence of ammonium. kcat is 25 min(-1) for the phosphorylation of pantothenate in the presence of ammonium.


organism: Rhodopseudomonas palustris

substrate_name: CoA

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

substrate: CoA


organism: Salmonella enterica

substrate_name: acetyl phosphate

assay_conditions_summary: 303.15 K; cofactor CoA

substrate: acetyl phosphate


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme

substrate: acetyl-CoA


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme


proof_lines: 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme


proof_lines: 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme


organism: Fructilactobacillus sanfranciscensis

assay_conditions_summary: cofactor CoA


organism: Lactococcus lactis subsp. cremoris

substrate_name: Acetyl phosphate; Coenzyme A

substrate: Acetyl phosphate; Coenzyme A


organism: Lactococcus lactis subsp. lactis

substrate_name: Coenzyme A; Acetyl phosphate

substrate: Coenzyme A; Acetyl phosphate


organism: Limosilactobacillus fermentum


organism: Methanosarcina thermophila


substrate_name: desulfo-CoA

substrate: desulfo-CoA


enzyme_display_name: Type III pantothenate kinase

organism: Bacillus subtilis (strain 168)

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

enzyme: Type III pantothenate kinase


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


enzyme_display_name: Pantothenate kinase 2, mitochondrial

organism: Homo sapiens

enzyme: Pantothenate kinase 2, mitochondrial


enzyme_display_name: Pantothenate kinase 3

substrate_name: ATP

enzyme: Pantothenate kinase 3

substrate: ATP


organism: Mus musculus

substrate_name: pantothenate


enzyme_display_name: Pantothenate kinase 1

enzyme: Pantothenate kinase 1


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature R133Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature C159S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature C312A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38503 and GenBank L23147/AAA72041.1

proof_lines:
wild-type after expression in E. coli
wild-type
wild type


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature R310Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C159A/C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines:
mutant R287Q
R287Q mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature R28Q to reconstruct the assayed variant sequence.

proof_lines:
mutant R28Q
R28Q mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C277A to reconstruct the assayed variant sequence.


enzyme_display_name: Xaa-Pro aminopeptidase

substrate_name: Arg-Pro-Pro

sequence_source: UniProtKB reviewed FASTA Q9NQW7

enzyme: Xaa-Pro aminopeptidase

substrate: Arg-Pro-Pro


substrate_name: H2O; Met-Pro-Ala

sequence_source: UniProtKB reviewed FASTA Q9NQH7

substrate: H2O; Met-Pro-Ala


substrate_name: Bradykinin

substrate: Bradykinin


substrate_name: H2O; Bradykinin

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9NQW7 and applied mutation signature R535A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Xaa-Pro aminopeptidase(Enzyme) mutant R535A His-tagged

proof_lines: pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride

substrate: H2O; Bradykinin


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9NQW7 and applied mutation signature Y527F to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: Xaa-Pro aminopeptidase(Enzyme) mutant Y527F His-tagged


organism: Streptomyces murinus

sequence_source: UniProtKB:A9E3K0 direct REST lookup on 2026-06-05

proof_lines:
native enzyme, pH 7.4, 30°C
recombinant enzyme, pH 7.4, 30°C


organism: Synechocystis sp. PCC 6803

sequence_source: UniProtKB:P74468 direct REST lookup on 2026-06-05


organism: Thermococcus onnurineus NA1

substrate_name: L-Met-L-Pro

sequence_source: UniProtKB:Q2QC92 direct REST lookup on 2026-06-05

substrate: L-Met-L-Pro


organism: Xanthomonas campestris

sequence_source: UniProtKB:Q8P5S7 direct REST lookup on 2026-06-05


organism: Deinococcus radiodurans

substrate_name: Arg-Pro-Ala

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUY4 canonical sequence fetched directly; R55A variant reconstructed from residue R55 to A. and applied mutation signature R55A to reconstruct the assayed variant sequence.

substrate: Arg-Pro-Ala


substrate_name: Met-Pro-Ala

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUY4 canonical sequence fetched directly; D53A variant reconstructed from residue D53 to A. and applied mutation signature D53A to reconstruct the assayed variant sequence.

substrate: Met-Pro-Ala


sequence_source: UniProtKB:Q9RUY4 canonical sequence fetched directly; R55A variant reconstructed from residue R55 to A.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUY4 canonical sequence fetched directly; Y56A variant reconstructed from residue Y56 to A. and applied mutation signature Y56A to reconstruct the assayed variant sequence.


substrate_name: Met-Pro

sequence_source: UniProtKB:Q9RUY4 canonical sequence fetched directly and used unchanged for wild type.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

substrate: Met-Pro


sequence_source: UniProtKB:Q9RUY4 canonical sequence fetched directly; D53A variant reconstructed from residue D53 to A.


organism: Escherichia coli

substrate_name: L-Ala-L-Pro-L-Ala

sequence_source: UniProtKB:P15034 canonical sequence fetched directly and used unchanged for wild type.

substrate: L-Ala-L-Pro-L-Ala


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST/FASTA I6YDN6, accessed 2026-06-05


substrate_name: Met-Ala-Ala

substrate: Met-Ala-Ala


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB REST/FASTA P40051, accessed 2026-06-05


substrate_name: Tyr-Ala-Ala

column_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3). Table 2, substrate row YAA; column Vmax (umol min^-1 mg^-1) = 1.5; column Km (mM) = 0.72; column Ki (mM) = 5 mM; column kcat (s^-1) = 1.4; column kcat/Km (M^-1 s^-1) (x 10^3) = 1.94. captured primary segment: YAA | Vmax 1.5 umol min^-1 mg^-1 | Km 0.72 mM | Ki 5 mM | kcat 1.4 s^-1 | kcat/Km 1.94 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.72 mM; the printed unit is already mM, so no unit conversion applies and the paper value is 0.72 mM. kcat: printed Table 2 kcat cell 1.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 1.4 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 1.94 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1940.0 x 0.001 = 1.94 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.4 / 0.72 = 1.9444444444444444 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.94 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row YAA: Km = 0.72 mM; kcat = 1.4 s^-1; printed kcat/Km = 1.94 x 10^3 M^-1 s^-1.

row_label: Table 2, substrate row YAA

substrate: Tyr-Ala-Ala


normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.72 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 0.72 mM. kcat: printed Table 2 kcat cell 1.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 1.4 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 1.94 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1940.0 x 0.001 = 1.94 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.4 / 0.72 = 1.9444444444444444 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.94 s^-1 mM^-1.

table_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3)


substrate_name: Tyr-Pro-Ala

column_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3). Table 2, substrate row YPA; column Vmax (umol min^-1 mg^-1) = 14.0; column Km (mM) = 1.8; column Ki (mM) = NA; column kcat (s^-1) = 14.0; column kcat/Km (M^-1 s^-1) (x 10^3) = 7.78. captured primary segment: YPA | Vmax 14.0 umol min^-1 mg^-1 | Km 1.8 mM | Ki NA | kcat 14.0 s^-1 | kcat/Km 7.78 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 1.8 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 1.8 mM. kcat: printed Table 2 kcat cell 14.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 14.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 7.78 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7780.0 x 0.001 = 7.78 s^(-1)*mM^(-1). Quotient disclosure for this row: 14.0 / 1.8 = 7.777777777777778 s^-1 mM^-1, against the printed catalytic-efficiency cell 7.78 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row YPA: Km = 1.8 mM; kcat = 14.0 s^-1; printed kcat/Km = 7.78 x 10^3 M^-1 s^-1.

row_label: Table 2, substrate row YPA

substrate: Tyr-Pro-Ala


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


organism: Caenorhabditis elegans

substrate_name: bradykinin

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

substrate: bradykinin


organism: Rattus norvegicus

substrate_name: Arg-Pro-Pro (at pH 8.0)

assay_conditions_summary: pH 8

substrate: Arg-Pro-Pro (at pH 8.0)


organism: Ashbya gossypii

sequence_source: UniProt Q75CD7 FASTA direct check 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProt Q9RUY4 FASTA plus Y56A reconstruction direct check 2026-06-05 and applied mutation signature Y56A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q9RUY4 FASTA direct check 2026-06-05


sequence_source: UniProt Q9RUY4 FASTA plus Y56A reconstruction direct check 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProt Q9RUY4 FASTA plus R55A reconstruction direct check 2026-06-05 and applied mutation signature R55A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9RUY4 FASTA plus D53A reconstruction direct check 2026-06-05 and applied mutation signature D53A to reconstruct the assayed variant sequence.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 8.6 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 5.4 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 5.5 and 37 degr


organism: Thermotoga maritima

substrate_name: CoA

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

substrate: CoA


organism: Veillonella parvula


substrate_name: L-tyrosine

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25°C

substrate: L-tyrosine


proof_lines: aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25°C


proof_lines: aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25°C


proof_lines: aspartate aminotransferase with mutations HEX, pH 8.0, 25°C


organism: Corynebacterium ammoniagenes

substrate_name: pantothenate

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines:
pH 6.5, 37°C
oxidized form, pH 6.5, 37°C
reduced form, pH 6.5, 37°C

substrate: pantothenate


substrate_name: (R)-Pantothenate; ATP

assay_conditions_summary: pH 8; 298.15 K; buffer form of MgATP2- Tris-HCl; cofactor ATP

proof_lines:
Tris-HCl buffer, pH 8.0
citrate buffer, pH 6.0
pH 7.4, 25°C

substrate: (R)-Pantothenate; ATP


organism: Helicobacter pylori

substrate_name: ATP

substrate: ATP


organism: Mus musculus

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant PANK1beta-3-1beta

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant PANK3-1beta-3


substrate_name: GTP

assay_conditions_summary: pH 6.5; buffer citrate; cofactor ATP

proof_lines: in citrate buffer, pH 6.5, temperature not specified in the publication

substrate: GTP


organism: Plasmodium falciparum

ki_unit: mM


organism: Papaver somniferum


organism: Prunella vulgaris

substrate_name: phenylpyruvate

proof_lines: with L-tyrosine as cosubstrate, at pH 8.0 and 30°C

proof_lines: with L-glutamate as cosubstrate, at pH 8.0 and 30°C

proof_lines: with 2-oxoglutarate as cosubstrate, at pH 8.0 and 30°C

substrate: phenylpyruvate


organism: Trichoderma viride


organism: Trypanosoma cruzi

substrate_name: pyruvate

proof_lines:
pH 7.0, 37°C, tyrosine as co-substrate
pH 7.0, 37°C, pyruvate as co-substrate

substrate: pyruvate


organism: Bacillus anthracis

substrate_name: dCTP

substrate: dCTP


organism: Bacillus subtilis


organism: Escherichia coli

substrate_name: L-Phenylalanine; 2-Oxoglutarate

substrate: L-Phenylalanine; 2-Oxoglutarate


organism: Felis catus


organism: Homo sapiens

substrate_name: L-glutamate

substrate: L-glutamate


organism: Oncorhynchus mykiss

proof_lines:
in liver
in white muscle


enzyme_display_name: dihydropteroate synthase

organism: Arabidopsis thaliana

sequence_source: UniProtKB Q1ENB6 REST direct check 2026-06-05

enzyme: dihydropteroate synthase


substrate_name: sulfanilamide

sequence_source: UniProtKB Q81VW8 REST direct check 2026-06-05

proof_lines:
in absence of 4-aminobenzoate
100 microM DHP-PP, 25 °C
20 microM DHP-PP, 25 °C

substrate: sulfanilamide


sequence_source: UniProtKB P0AC13 REST direct check 2026-06-05


organism: Escherichia coli MC4100


organism: Mycobacterium leprae

sequence_source: UniProtKB P0C0X1 REST direct check 2026-06-05


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WND1 REST direct check 2026-06-05


organism: Rattus norvegicus

substrate_name: ATP; (R)-Pantothenate

proof_lines:
pH 7.0, 37°C
ATP in form of MgATP2-
pH 6.1, 37°C

substrate: ATP; (R)-Pantothenate


organism: Spinacia oleracea

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines:
isoform 1, 37°C, pH 8.0
isoform 2, 37°C, pH 8.0


organism: Staphylococcus aureus

sequence_source: UniProtKB reviewed Q2FWC7; direct lit_pubmed:15548531 EC+organism lookup.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, recombinant enzyme
pH 7.5, 25°C


organism: Thermotoga maritima

substrate_name: (R)-pantothenate

sequence_source: UniProtKB reviewed Q9WZY5; direct lit_pubmed:16855243 structural PanK-III lookup.

assay_conditions_summary: pH 7.6; 323.15 K; cofactor ATP

proof_lines: in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50°C

substrate: (R)-pantothenate


organism: Haemophilus influenzae

sequence_source: UniProtKB reviewed P43890; direct lit_pubmed:17210578 EC+organism lookup.

proof_lines: in presence of 1.0 mM UMP and 0.5 mM GTP

proof_lines: in presence of 1.0 mM ATP and 0.5 mM GTP


organism: Saccharolobus solfataricus

sequence_source: UniProtKB reviewed Q97ZE2; direct lit_pubmed:17297917 structural uridylate kinase lookup.

assay_conditions_summary: 333.15 K; cofactor ATP

proof_lines:
in presence of 0.1 mM UMP, at 60°C
in presence of 0.5 mM ATP at 60°C
in presence of 0.5 mM ATP


organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 canonical sequence reconstructed with RCSB/PDB 6JWS mutation A437G and applied mutation signature A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 canonical sequence reconstructed with RCSB/PDB 6KCL mutations A437G,K540E and applied mutation signature A437G/K540E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A437G/K540E, at pH 9.0 and 37°C


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:Q25704 canonical sequence

source: skid


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P53848 canonical sequence

proof_lines: recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase


substrate_name: p-Aminobenzoic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence reconstructed with source mutation note T557A and applied mutation signature T557A to reconstruct the assayed variant sequence.

substrate: p-Aminobenzoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence reconstructed with source mutation note T557A/P559S and applied mutation signature T557A/P559S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence reconstructed with source mutation note P559S and applied mutation signature P559S to reconstruct the assayed variant sequence.


organism: Pisum sativum


organism: Pneumocystis carinii


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature S436A/A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature A613T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature S436F/A437G/A613T to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature S436F/A437G/A613S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature K540E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature A437G/K540E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P9WND1 direct FASTA/JSON lookup on 2026-06-05

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_source: UniProtKB:O04862 direct FASTA/JSON lookup on 2026-06-05


sequence_source: UniProtKB:Q25704 direct FASTA/JSON lookup on 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 direct FASTA/JSON lookup plus local A613S reconstruction on 2026-06-05 and applied mutation signature A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 direct FASTA/JSON lookup plus local A437G reconstruction on 2026-06-05 and applied mutation signature A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 direct FASTA/JSON lookup plus local S436F/A613S reconstruction on 2026-06-05 and applied mutation signature S436F/A613S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436F/A613S, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence with source-stated T557V/P559S substitutions applied after residue check and applied mutation signature T557V/P559S to reconstruct the assayed variant sequence.


proof_lines:
wild type
wild tpye


sequence_source: UniProtKB:O05701 canonical sequence


organism: Streptococcus pneumoniae

sequence_source: UniProtKB:P05382 canonical sequence

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.


sequence_source: UniProtKB:P05382 canonical sequence checked as context only; row-specific variant sequence not resolved

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: dihydropteroate synthase(Enzyme) mutant


organism: Streptococcus pyogenes

sequence_source: UniProtKB:P0C0G1 canonical sequence


sequence_source: UniProtKB:P0C0G0 canonical sequence


organism: Escherichia coli

sequence_source: UniProtKB:P15034 canonical sequence checked as context only; H350A coordinate did not match canonical residue 350


substrate_name: Met-Pro-Ala

substrate: Met-Pro-Ala


substrate_name: Met-Pro

substrate: Met-Pro


substrate_name: Met-Ala-Ala

substrate: Met-Ala-Ala


organism: Gibberella zeae

substrate_name: Met-Pro-Ala; H2O

substrate: Met-Pro-Ala; H2O


organism: Homo sapiens

substrate_name: bradykinin

proof_lines: pH 8.2, 37°C, recombinant wild-type enzyme

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme

substrate: bradykinin


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature S436F/A613T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436F/A613T, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature A581G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature S436F/A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature S436A/A437G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436A/A437G, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature K540E to reconstruct the assayed variant sequence.


substrate_name: 4-aminobenzoate (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 0.46 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.28 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).


proof_lines: kcat is 0.38 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.26 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).

substrate: 4-aminobenzoate (at pH 7.5 and 37 degrees Celsius)


proof_lines: kcat is 0.42 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.25 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).


organism: Escherichia coli (strain K12)

proof_lines: kcat is 0.38 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.46 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).


organism: Mycobacterium leprae (strain TN)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 35 min(-1) (PubMed:10542185). kcat is 28 min(-1) with pABA as substrate, and 45 min(-1) with PAS as substrate (PubMed:23118010).


substrate_name: ATP

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

proof_lines: in presence of 1.0 mM UMP and 0.5 mM GTP

substrate: ATP


substrate_name: apo-[Streptomyces sp. granaticin-acyl-carrier protein]

proof_lines:
pH 7.0, 37°C, E. coli ACP
pH 8.8, 37°C
pH 8.8, 37°C, 250 mM NaCl


substrate_name: apo-ACP

proof_lines: pH 7.0, 37°C, Bacillus subtilis acyl carrier protein-A as substrate

proof_lines: pH 7.0, 37°C, human acyl carrier protein f as as substrate

proof_lines: pH 7.0, 37°C, human acyl carrier protein mit as substrate

substrate: apo-ACP


organism: Mycoplasmoides pneumoniae

substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

substrate: crotonyl-CoA


organism: Pseudomonas aeruginosa

substrate_name: CoA

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C

proof_lines: in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C

substrate: CoA


organism: Pseudomonas putida

substrate_name: apo-[BpsA protein]

substrate: apo-[BpsA protein]


organism: Campylobacter jejuni

proof_lines:
sulfonamide resistant enzyme
resistant enzyme


substrate_name: sulfathiazole

substrate: sulfathiazole


organism: Lactiplantibacillus plantarum

substrate_name: Unknown

substrate: Unknown


organism: Lathyrus oleraceus

proof_lines: inhibitor of 6-hydroxymethyl-7,8-dihydropteridine diphosphate


organism: Plasmodium berghei


organism: Plasmodium chabaudi


organism: Plasmodium vivax

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


proof_lines: mutant enzyme S382A/A383G/A553G, pH 9.0, 37°C


organism: Streptococcus pneumoniae


organism: Staphylococcus aureus

substrate_name: UMP

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines:
pH 7.5, 22°C, ordered BiBi mechanism
in presence of 1.0 mM UMP without GTP
pH 7.5, 22°C, random BiBi mechanism

substrate: UMP


organism: Spinacia oleracea

substrate_name: apo-acyl-carrier protein

substrate: apo-acyl-carrier protein


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


organism: Streptomyces pneumoniae

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines: pH 7.0, 37°C, trichloroacetic acid precipitation method


enzyme_display_name: licheninase

organism: Bacillus sp. (in: firmicutes)

substrate_name: Laminarin

enzyme: licheninase

substrate: Laminarin


organism: Plasmodium falciparum


substrate_name: lichenan

substrate: lichenan


enzyme_display_name: fatty acid amide hydrolase

organism: Unknown

enzyme: fatty acid amide hydrolase


organism: Rattus norvegicus

substrate_name: oleamide ((9Z)-octadecenamide)

proof_lines: kcat is 7.1 sec(-1) with oleamide ((9Z)-octadecenamide) (PubMed:9790682). kcat is 28 min(-1) with 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:17649977). kcat is 16 min(-1) with anandamide (N-(5Z,8Z,11Z,14Z-e

substrate: oleamide ((9Z)-octadecenamide)


organism: Arabidopsis thaliana

substrate_name: N-acylethanolamine 20:4

substrate: N-acylethanolamine 20:4


organism: Caenorhabditis elegans


organism: Homo sapiens


organism: Sus scrofa


organism: Bacillus tequilensis

substrate_name: azo blue barley beta-glucan

proof_lines: mutant N31C/T187C/P102C/N125C, at pH 6.5 and 40°C

substrate: azo blue barley beta-glucan


substrate_name: Barley beta-glucan

substrate: Barley beta-glucan


organism: Bispora sp. MEY-1

substrate_name: lichenin

substrate: lichenin


substrate_name: Barley glucan

substrate: Barley glucan


organism: Fibrobacter succinogenes


organism: Bacillus sp. SJ-10


organism: Bacillus subtilis


proof_lines:
wild-type, pH 6.5, 40°C
wild type enzyme, at pH 6.5 and 40°C


sequence_source: UniProtKB P17989 canonical sequence; M39F reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature M39F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P17989 canonical sequence; D58N reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature D58N matches the mutant residue at offset +9 and the reference residue at offset +15; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P17989 canonical sequence; G63A reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature G63A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P17989 canonical sequence; E56D reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature E56D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P17989 canonical sequence for Fibrobacter succinogenes beta-glucanase, EC 3.2.1.73.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines:
wild type
pH 6.0, 40°C, wild type


proof_lines:
expressed in Pichia pastoris
expressed in Escherichia coli


substrate_name: Palmitoylethanolamide

sequence_source: UniProtKB REST Q7XJJ7 and identity reuse cache accession:Q7XJJ7

smiles: CCCCCCCCCCCCCCCC(O)=NCCO

substrate: Palmitoylethanolamide


substrate_name: Dodecanoyl ethanolamide

smiles: CCCCCCCCCCCC(=O)NCCO

substrate: Dodecanoyl ethanolamide


substrate_name: Linoleoylethanolamide

smiles: CCCCCC=CCC=CCCCCCCCC(=O)NCCO

substrate: Linoleoylethanolamide


substrate_name: Anandamide

substrate: Anandamide


substrate_name: H2O; Anandamide

proof_lines:
at 9.0 pH and 30°C
at pH 9.0 and 30°C

substrate: H2O; Anandamide


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB REST O00519, identity reuse cache accession:O00519, and selected BRENDA P129T note and applied mutation signature P129T to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_source: UniProtKB REST O00519 and identity reuse cache accession:O00519


substrate_name: Anandamide; H2O

sequence_source: UniProtKB REST P97612 and identity reuse cache accession:P97612

proof_lines:
at 9.0 pH and 30°C
at pH 9.0 and 30°C
pH 9.0, 22°C

substrate: Anandamide; H2O


organism: Secale cereale

substrate_name: H2O; DIBOA glucoside

sequence_source: UniProtKB Q9FYS3 FASTA/JSON direct check, 2026-06-05

proof_lines: pH and temperature not specified in the publication

substrate: H2O; DIBOA glucoside


substrate_name: DIBOA glucoside

sequence_variant_note: Mutation signature Y378F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: DIBOA glucoside


substrate_name: DIMBOA glucoside

sequence_variant_note: Mutation signature G464F matches the mutant residue at offset -11 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: DIMBOA glucoside


sequence_variant_note: Mutation signature F198A matches the mutant residue at offset +2 and the reference residue at offset +10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: DIBOA glucoside; H2O

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant F471Y His-tagged

substrate: DIBOA glucoside; H2O


proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant G464F His-tagged


sequence_variant_note: Mutation signature S465L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Triticum aestivum

sequence_source: Canonical context only from UniProtKB reviewed accession Q1XIR9 (HGL1A_WHEAT) direct REST check, 2026-06-05

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant F198 His-tagged


sequence_source: Reconstructed from UniProtKB reviewed accession Q1XIR9 (HGL1A_WHEAT) plus PMID 16751439 mutation label Y378F


substrate_name: DIBOA-glucoside

sequence_source: Reconstructed from UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) plus PMID 16751439 mutation label S464F

sequence_variant_note: Mutation signature S464F matches the mutant residue at offset -11 and the reference residue at offset +3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: DIBOA-glucoside


sequence_source: UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) direct REST check, 2026-06-05


substrate_name: DIMBOA-glucoside

sequence_source: Reconstructed from UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) plus PMID 16751439 mutation label Y378A

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.

substrate: DIMBOA-glucoside


sequence_source: Reconstructed from UniProtKB reviewed accession Q1XIR9 (HGL1A_WHEAT) plus PMID 16751439 mutation label F471Y


substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_source: Reconstructed from UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) plus PMID 16751439 mutation label F198A

substrate: 4-nitrophenyl beta-D-glucoside


column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1b', DIMBOA-Glc block; column 'Km (mM)' = 0.29; column 'kcat (s^-1)' = 1,201; column 'kcat/Km (s^-1/mM)' = 4,138.

normalized_value_unit_evidence: kcat: printed Table II cell 1,201 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 1201.0 s^(-1). Km: printed cell 0.29 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 0.29 mM. kcat/Km: printed cell 4,138 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 4138.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1b, DIMBOA-Glc block: Km cell 0.29 mM; kcat cell 1,201 s^-1; printed kcat/Km cell 4,138 s^-1/mM.

row_label: Table II, row TaGlu1b, DIMBOA-Glc block


sequence_source: UniProtKB Q1XIR9 canonical sequence fetched 2026-06-05 by direct accession lookup.

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.


sequence_source: UniProtKB Q1XH04 canonical sequence fetched 2026-06-05 by direct accession lookup.

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1c', DIMBOA-Glc block; column 'Km (mM)' = 0.39; column 'kcat (s^-1)' = 773; column 'kcat/Km (s^-1/mM)' = 1979.

normalized_value_unit_evidence: kcat: printed Table II cell 773 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 773.0 s^(-1). Km: printed cell 0.39 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 0.39 mM. kcat/Km: printed cell 1979 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 1979.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1c, DIMBOA-Glc block: Km cell 0.39 mM; kcat cell 773 s^-1; printed kcat/Km cell 1979 s^-1/mM.

row_label: Table II, row TaGlu1c, DIMBOA-Glc block


sequence_source: UniProtKB Q1XH05 canonical sequence fetched 2026-06-05; row-specific Y378F variant reconstructed with checked UniProt residue 427.


sequence_source: UniProtKB Q1XIR9 canonical sequence fetched 2026-06-05; row-specific Y378F variant reconstructed with checked UniProt residue 427.


sequence_source: UniProtKB Q1XH05 canonical sequence fetched 2026-06-05; row-specific S464F variant reconstructed with checked UniProt residue 513.


sequence_source: UniProtKB Q1XH05 canonical sequence fetched 2026-06-05 by direct accession lookup.


sequence_source: UniProtKB reviewed entry Q1XH05 (HGL1B_WHEAT) direct REST FASTA/JSON check


sequence_source: UniProtKB reviewed entry Q1XH04 (HGL1C_WHEAT) direct REST FASTA/JSON check

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1c', DIBOA-Glc block; column 'Km (mM)' = 1.05; column 'kcat (s^-1)' = 137; column 'kcat/Km (s^-1/mM)' = 131.

normalized_value_unit_evidence: kcat: printed Table II cell 137 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 137.0 s^(-1). Km: printed cell 1.05 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 1.05 mM. kcat/Km: printed cell 131 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 131.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1c, DIBOA-Glc block: Km cell 1.05 mM; kcat cell 137 s^-1; printed kcat/Km cell 131 s^-1/mM.

row_label: Table II, row TaGlu1c, DIBOA-Glc block


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q1XIR9 (HGL1A_WHEAT) direct REST FASTA/JSON check and applied mutation signature S464F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant S464F His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05 canonical sequence; variant reconstructed from selected mutation_signature Y378A and applied mutation signature Y378A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature S464F

sequence_variant_note: Mutation signature S464F matches the mutant residue at offset -11 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:Q1XIR9 canonical sequence

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1a', DIBOA-Glc block; column 'Km (mM)' = 1.40; column 'kcat (s^-1)' = 48.8; column 'kcat/Km (s^-1/mM)' = 34.6.

normalized_value_unit_evidence: kcat: printed Table II cell 48.8 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 48.8 s^(-1). Km: printed cell 1.40 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 1.4 mM. kcat/Km: printed cell 34.6 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 34.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1a, DIBOA-Glc block: Km cell 1.40 mM; kcat cell 48.8 s^-1; printed kcat/Km cell 34.6 s^-1/mM.

row_label: Table II, row TaGlu1a, DIBOA-Glc block


sequence_source: UniProtKB:Q1XH05 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05 canonical sequence; variant reconstructed from selected mutation_signature F471Y and applied mutation signature F471Y with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature Y378F and applied mutation signature Y378F with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Y378F His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature Y378A and applied mutation signature Y378A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Y378A His-tagged


sequence_source: UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature Y378A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature G464S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature F198A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant F198A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature G464S/S465L with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature Y378F with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature S465L with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant S465L His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature Y378A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3; reconstructed F471Y variant as canonical residue F520Y with +49 offset and applied mutation signature F471Y with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3; reconstructed Y378F variant as canonical residue Y427F with +49 offset and applied mutation signature Y378F with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3; reconstructed G464S variant as canonical residue G513S with +49 offset and applied mutation signature G464S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant G464S His-tagged


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


substrate_name: DIMBOA glucoside; H2O

substrate: DIMBOA glucoside; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05; reconstructed F198A variant as canonical residue F247A with +49 offset and applied mutation signature F198A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05; reconstructed F471Y variant as canonical residue F520Y with +49 offset and applied mutation signature F471Y with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1XIR9; reconstructed S464F variant as canonical residue S513F with +49 offset


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_source: UniProtKB reviewed accession Q1XH05

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


organism: Zea mays

substrate_name: H2O; DIMBOA glucoside

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Chim 2

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Chim 15

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Chim 16

substrate: H2O; DIMBOA glucoside


sequence_source: UniProtKB reviewed accession P49235


sequence_source: UniProtKB:P49235 direct REST lookup; reviewed Swiss-Prot HGGL1_MAIZE


substrate_name: p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)


enzyme_display_name: methylthioadenosine nucleosidase

organism: Brucella melitensis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8YBL1 FASTA direct lookup; M144A reconstructed after residue M144 matched the canonical sequence. and applied mutation signature M144A to reconstruct the assayed variant sequence.

enzyme: methylthioadenosine nucleosidase