sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Hexanoyl-CoA; F265V column group; kcat cell = 3.56 min^-1; Km cell = 5.0 uM; kcat/Km cell = 11,866 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.56 min^-1; the printed turnover column is per MINUTE, so 3.56 / 60 = 0.059333333333333335 s^-1; the exported value is 3.56 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.0 uM; 1 uM = 1/1000 mM, so 5.0 / 1000 = 0.005 mM; the exported value is 5.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 11,866 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 11,866 / 1000 = 11.866 s^-1 mM^-1; the exported value is 11866.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Hexanoyl-CoA: kcat = 3.56 min^-1; Km = 5.0 uM; kcat/Km = 11,866 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


enzyme_display_name: chalcone synthase

organism: Medicago sativa

substrate_name: Phenylacetyl-CoA

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Phenylacetyl-CoA; F265V column group; kcat cell = 4.37 min^-1; Km cell = 5.7 uM; kcat/Km cell = 12,778 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.37 min^-1; the printed turnover column is per MINUTE, so 4.37 / 60 = 0.07283333333333333 s^-1; the exported value is 4.37 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.7 uM; 1 uM = 1/1000 mM, so 5.7 / 1000 = 0.0057 mM; the exported value is 5.7 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 12,778 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 12,778 / 1000 = 12.778 s^-1 mM^-1; the exported value is 12778.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Phenylacetyl-CoA: kcat = 4.37 min^-1; Km = 5.7 uM; kcat/Km = 12,778 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.

data_origin: experimental

enzyme: chalcone synthase

substrate: Phenylacetyl-CoA

status: corrected

source: oed


substrate_name: Feruloyl-CoA

mutation_signature: Unknown

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

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Feruloyl-CoA; CHS column group; kcat cell = 1.04 min^-1; Km cell = 5.2 uM; kcat/Km cell = 3,333 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.04 min^-1; the printed turnover column is per MINUTE, so 1.04 / 60 = 0.017333333333333333 s^-1; the exported value is 1.04 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.2 uM; 1 uM = 1/1000 mM, so 5.2 / 1000 = 0.0052 mM; the exported value is 5.2 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 3,333 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 3,333 / 1000 = 3.333 s^-1 mM^-1; the exported value is 3333.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, CHS column group, substrate row Feruloyl-CoA: kcat = 1.04 min^-1; Km = 5.2 uM; kcat/Km = 3,333 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.

substrate: Feruloyl-CoA


column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Feruloyl-CoA; F265V column group; kcat cell = 2.43 min^-1; Km cell = 9.0 uM; kcat/Km cell = 4,500 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.43 min^-1; the printed turnover column is per MINUTE, so 2.43 / 60 = 0.0405 s^-1; the exported value is 2.43 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 9.0 uM; 1 uM = 1/1000 mM, so 9.0 / 1000 = 0.009 mM; the exported value is 9.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 4,500 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 4,500 / 1000 = 4.5 s^-1 mM^-1; the exported value is 4500.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Feruloyl-CoA: kcat = 2.43 min^-1; Km = 9.0 uM; kcat/Km = 4,500 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


substrate_name: Octanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Octanoyl-CoA; F265V column group; kcat cell = 9.82 min^-1; Km cell = 5.6 uM; kcat/Km cell = 29,226 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.82 min^-1; the printed turnover column is per MINUTE, so 9.82 / 60 = 0.16366666666666668 s^-1; the exported value is 9.82 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.6 uM; 1 uM = 1/1000 mM, so 5.6 / 1000 = 0.0056 mM; the exported value is 5.6 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 29,226 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 29,226 / 1000 = 29.226 s^-1 mM^-1; the exported value is 29226.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Octanoyl-CoA: kcat = 9.82 min^-1; Km = 5.6 uM; kcat/Km = 29,226 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.

substrate: Octanoyl-CoA


organism: Sorbus aucuparia

substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

kcat_over_km_display: Not reported

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

sequence_source: UniProtKB Q27Z06 direct REST lookup; EMBL DQ286037 protein ABB89213.1; reference PMID 17109150

assay_conditions_summary: cofactor CoA

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


verification_status: unverified

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7; 308.15 K; cofactor CoA

status: unverified


verification_status: verified

sequence_source: UniProtKB:P30074 REST lookup on 2026-06-05

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row o-Coumaroyl-CoA; kcat column raw 2.32 min^-1; Km column raw 3.8 uM; kcat/Km column raw 10,175 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 2.32 min^-1 / 60 = 0.038667 s^-1, carried at the export precision as normalized_value=0.039 normalized_unit=s^-1; Km 3.8 uM / 1000 = 0.003800 mM, carried at the export precision as normalized_value=0.004 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 9.75 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 10,175 M^-1 s^-1 normalizes to 10.175 s^-1*mM^-1 (deviation 4.2%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row o-Coumaroyl-CoA: kcat raw_value=2.32 raw_unit=min^-1; Km raw_value=3.8 raw_unit=uM; kcat/Km raw_value=10,175 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | o-Coumaroyl-CoA

status: verified


substrate_name: Cinnamoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Cinnamoyl-CoA; kcat column raw 4.76 min^-1; Km column raw 5.0 uM; kcat/Km column raw 15,866 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 4.76 min^-1 / 60 = 0.079333 s^-1, carried at the export precision as normalized_value=0.079 normalized_unit=s^-1; Km 5.0 uM / 1000 = 0.005000 mM, carried at the export precision as normalized_value=0.005 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 15.8 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 15,866 M^-1 s^-1 normalizes to 15.866 s^-1*mM^-1 (deviation 0.4%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row Cinnamoyl-CoA: kcat raw_value=4.76 raw_unit=min^-1; Km raw_value=5.0 raw_unit=uM; kcat/Km raw_value=15,866 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | Cinnamoyl-CoA

substrate: Cinnamoyl-CoA


substrate_name: phenylpropionyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row 3-Phenylpropionyl-CoA; literal cells kcat 4.95 min^-1, Km 4.9 uM, kcat/Km 16,836 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 4.95 min^-1 normalizes to 0.0825 s^-1 and is stored at current precision as 0.083; printed Km 4.9 uM normalizes to 0.004900000000000001 mM and is stored as 0.005; current stored quotient is 16.6 s^-1*mM^-1; the independently printed ratio normalizes to 16.836 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row 3-Phenylpropionyl-CoA: kcat 4.95 min^-1; Km 4.9 uM; kcat/Km 16,836 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | 3-Phenylpropionyl-CoA

substrate: phenylpropionyl-CoA


substrate_name: n-Valeryl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Valeryl-CoA', F265V column group; column 'kcat (min^-1)' = 1.33; column 'Km (uM)' = 6.1; column 'kcat/Km (M^-1 s^-1)' = 3,634.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Valeryl-CoA: kcat = 1.33 min^-1; Km = 6.1 uM; printed kcat/Km = 3,634 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Valeryl-CoA'

table_label: Table 2. Steady-state kinetic parameters (Proc. Natl. Acad. Sci. U.S.A. 2002, 99(8): 5319-5324, journal page 5321)

substrate: n-Valeryl-CoA


organism: Panicum virgatum

source_db: brenda

sequence_source: UniProtKB:A0A8T0PQ54 REST lookup on 2026-06-05

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

proof_lines: in the presence of chalcone isomerase and chalcone isomerase-like protein, pH and temperature not specified in the publication

proof_lines: in the presence of chalcone isomerase, pH and temperature not specified in the publication

proof_lines: in the presence of chalcone isomerase-like protein, pH and temperature not specified in the publication

source: brenda


organism: Physcomitrium patens

substrate_name: p-Coumaroyl-CoA; malonyl-CoA

kcat_display: Not reported

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

sequence_source: UniProtKB:Q2VAZ3 REST lookup on 2026-06-05

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

proof_lines:
37°C, pH 7.2
Raw SKiD Env: Temp=37°C, pH=7.2

source_databases_merged: brenda skid

substrate: p-Coumaroyl-CoA; malonyl-CoA


organism: Polygonum cuspidatum

substrate_name: malonyl-CoA; 4-coumaroyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:H9DV62 canonical sequence with R105Q reconstructed on 2026-06-05 and applied mutation signature R105Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication

substrate: malonyl-CoA; 4-coumaroyl-CoA


substrate_name: 4-coumaroyl-CoA; malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:H9DV62 canonical sequence with Q82P reconstructed on 2026-06-05 and applied mutation signature Q82P to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication

substrate: 4-coumaroyl-CoA; malonyl-CoA


sequence_source: UniProtKB:H9DV62 direct REST lookup on 2026-06-05

proof_lines: wild type enzyme, at pH 8.0, temperature not specified in the publication


substrate_name: malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:H9DV62 direct REST lookup on 2026-06-05 plus row mutation Q82P/C198F and applied mutation signature Q82P/C198F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication

substrate: malonyl-CoA


organism: Rheum australe

substrate_name: octanoyl-CoA

km_display: Not reported

sequence_source: UniProtKB:A0A096X8J8 direct REST lookup on 2026-06-05

proof_lines: isoform CHS1, pH and temperature not specified in the publication

substrate: octanoyl-CoA


sequence_source: UniProtKB:A0A0A0P7Q3 direct REST lookup on 2026-06-05

proof_lines: isoform CHS2, pH and temperature not specified in the publication


organism: Rubus idaeus

sequence_source: UniProtKB:Q9AU11 direct REST lookup on 2026-06-05

assay_conditions_summary: pH 9.5; 308.15 K; cofactor CoA


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

assay_conditions_summary: pH 7.5; 313.15 K; cofactor CoA


sequence_source: UniProtKB:Q8L5L2 direct REST lookup on 2026-06-05


enzyme_display_name: catalase

organism: Brassica oleracea

proof_lines:
isoenzyme with optimum at pH 4.5
isoenzyme with optimum at pH 6.5
isoenzyme with optimum at pH 10.0

enzyme: catalase


organism: Cytobacillus firmus

proof_lines:
isoenzyme II
isoenzyme I


organism: Escherichia coli

proof_lines: presence of 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.0

proof_lines: presence of 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.5


enzyme_display_name: bacterial leucyl aminopeptidase

organism: Vibrio proteolyticus

sequence_source: UniProtKB Q01693 canonical FASTA checked directly by UniProt REST.

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tricine

proof_lines: wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C

enzyme: bacterial leucyl aminopeptidase


substrate_name: H2O; L-Leucinyl-p-nitroanilide

sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; E151D reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 257 E with D. and applied mutation signature E151D with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bacterial leucyl aminopeptidase(Enzyme) mutant E151D-AAP

substrate: H2O; L-Leucinyl-p-nitroanilide


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

sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; E151H reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 257 E with H. and applied mutation signature E151H with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bacterial leucyl aminopeptidase(Enzyme) mutant E151H-AAP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; M180A reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 286 M with A. and applied mutation signature M180A with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; S228A reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 334 S with A. and applied mutation signature S228A with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; D118N reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 224 D with N. and applied mutation signature D118N with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; D99M reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 205 D with M. and applied mutation signature D99M with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 10 mM Tricine

proof_lines: apparent value, mutant enzyme D99M, in 10 mM Tricine buffer, pH 8.0, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F265V to reconstruct the assayed variant sequence.


substrate_name: Hexanoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F215S to reconstruct the assayed variant sequence.

substrate: Hexanoyl-CoA


substrate_name: N-Methylanthraniloyl-CoA

substrate: N-Methylanthraniloyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: heptanoyl-CoA

substrate: heptanoyl-CoA


substrate_name: Benzoyl-CoA

substrate: Benzoyl-CoA


organism: Spinacia oleracea

proof_lines:
isozyme AII
isozyme AI


organism: Unknown

substrate_name: L-leucine 4-nitroanilide

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

substrate: L-leucine 4-nitroanilide


organism: Humulus lupulus

source_db: uniprot

source: uniprot


organism: Hypericum androsaemum


organism: Bacillus subtilis (strain 168)

substrate_name: Arg-pNA

substrate: Arg-pNA


organism: Bacillus subtilis

substrate_name: hydrogen peroxide

substrate: hydrogen peroxide


organism: Lentzea aerocolonigenes

proof_lines: kcat is 64000 min(-1) for 2-imino-3-(indol-3-yl)propanoate (at pH 7.5).


organism: Oryza sativa subsp. japonica

proof_lines: kcat is 6.6 min(-1) with H(2)O(2) as substrate (at pH 7.5).


proof_lines: kcat is 20 min(-1) with H(2)O(2) as substrate (at pH 7.5).


substrate_name: H(2)O(2) (at pH 7.4 and 30 degrees Celsius)

proof_lines: kcat is 0.5 min(-1) with H(2)O(2) as substrate (at pH 7.5) (PubMed:21979082). kcat is 28 sec(-1) with H(2)O(2) as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:26900141).


proof_lines: kcat is 0.21x10(-3) sec(-1) with 4-coumaroyl-CoA as substrate (PubMed:29760092). kcat is 0.24x10(-3) sec(-1) with malonyl-CoA as substrate (PubMed:29760092). kcat is 1.2x10(-3) sec(-1) with 4-coumaroyl-CoA as substrate (in the presence of C


substrate_name: L-Arginyl-p-nitroanilide; H2O

sequence_source: UniProtKB P25152 direct accession lookup; reviewed Bacillus subtilis strain 168 BSAP/aminopeptidase sequence checked 2026-06-05

substrate: L-Arginyl-p-nitroanilide; H2O


sequence_source: UniProtKB O32106 direct accession lookup; reviewed Bacillus subtilis strain 168 aminopeptidase sequence checked 2026-06-05

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


organism: Geobacillus stearothermophilus

sequence_variant_note: Resolved canonical sequence from UniProtKB P24828 direct accession lookup plus H227L substitution reconstructed against the canonical sequence on 2026-06-05 and applied mutation signature H227L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P24828 direct accession lookup plus H191L substitution reconstructed against the canonical sequence on 2026-06-05 and applied mutation signature H191L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P24828 direct accession lookup; reviewed Geobacillus stearothermophilus aminopeptidase 2 sequence checked 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 Q01693 direct accession lookup checked 2026-06-05; canonical sequence retained as context only because E151Q could not be safely reconstructed from full-sequence numbering

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: bacterial leucyl aminopeptidase(Enzyme) mutant E151Q


substrate_name: Met-Leu-p-nitroanilide

sequence_source: UniProtKB Q01693 direct accession lookup; reviewed Vibrio proteolyticus bacterial leucyl aminopeptidase sequence checked 2026-06-05

substrate: Met-Leu-p-nitroanilide


substrate_name: H2O; Met-Leu-p-nitroanilide

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

proof_lines: pH 8.0, 37°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)

proof_lines: pH 8.0, 37°C, recombinant His6-tagged enzyme, without preincubation

source_databases_merged: sabio_rk brenda skid

substrate: H2O; Met-Leu-p-nitroanilide


enzyme_display_name: nitronate monooxygenase

organism: Neurospora crassa

sequence_source: UniProtKB reviewed accession Q01284 FASTA, retrieved 2026-06-05

enzyme: nitronate monooxygenase


smiles: O=O


smiles: CCCCCC[N+](=O)[O-]


substrate_name: O2; 2-Nitropropane

proof_lines: pH and temperature not specified in the publication

substrate: O2; 2-Nitropropane


substrate_name: nitroethane

substrate: nitroethane


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)


organism: Aspergillus niger

substrate_name: 2-Nitropropane; O2

substrate: 2-Nitropropane; O2


organism: Cyberlindnera mrakii

sequence_source: UniProtKB direct accession check: Q12723 reviewed Swiss-Prot entry 2NPD_CYBMR

proof_lines:
anionic form of the substrate
neutral form of the substrate


organism: Metarhizium brunneum

sequence_source: UniProtKB direct accession check: A0A6C0WWH2 unreviewed TrEMBL entry A0A6C0WWH2_9HYPO


substrate_name: ethyl nitronate

sequence_source: UniProtKB direct accession check: Q01284 reviewed Swiss-Prot entry 2NPD_NEUCR

substrate: ethyl nitronate


organism: Anopheles gambiae


proof_lines:
pH 7.0, 25°C, immobilized enzyme
pH 7.0, 25°C, free enzyme


organism: Bacillus anthracis

proof_lines: recombinant wild-type enzyme, pH 7.0, 25°C


organism: Bacillus pumilus


organism: Bacillus sp. (in: firmicutes)

assay_conditions_summary: pH 8.5; 277.15 K; buffer conditions

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), at 4°C

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), at 25°C


organism: Beta vulgaris subsp. cicla


organism: Bos taurus

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7

proof_lines: free catalase, in 50 mM phosphate buffer pH 7.0, at 25°C


organism: Brassica oleracea var. gongylodes

proof_lines:
first isoform, 25°C, pH 4.5
second isoform, 25°C, pH 6.5
third isoform, 25°C, pH 10.0


sequence_source: UniProtKB reviewed entry Q01284, retrieved 2026-06-05


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed entry Q9HWH9, retrieved 2026-06-05


substrate_name: ethylnitronate

substrate: ethylnitronate


organism: Williopsis mrakii

sequence_source: UniProtKB reviewed entry Q12723, retrieved 2026-06-05


enzyme_display_name: catechol oxidase

organism: Portulaca grandiflora

substrate_name: L-Dopa

proof_lines:
isoenzyme Ia
isoenzyme Ib
isoenzyme II

enzyme: catechol oxidase

substrate: L-Dopa


organism: Prunus persica

substrate_name: catechol

proof_lines:
isoenzyme C
isoenzyme D
isoenzyme A

substrate: catechol


organism: Ipomoea batatas

sequence_source: UniProtKB direct accession lookup Q9ZP19 via rest.uniprot.org/uniprotkb/Q9ZP19.json on 2026-06-05


substrate_name: caffeic acid

sequence_source: UniProtKB direct accession lookup B5M680 via rest.uniprot.org/uniprotkb/B5M680.json on 2026-06-05

substrate: caffeic acid


substrate_name: chlorogenic acid

sequence_source: UniProtKB direct accession lookup Q5ENY2 via rest.uniprot.org/uniprotkb/Q5ENY2.json on 2026-06-05

substrate: chlorogenic acid


organism: Mangifera indica

sequence_source: UniProtKB direct accession lookup D2XZ13 via rest.uniprot.org/uniprotkb/D2XZ13.json on 2026-06-05

proof_lines:
pH 6.2, 25°C, sodium phosphate buffer
pH 5.8, 25°C, sodium phosphate buffer
pH 5.8, 25°C


organism: Solanum lycopersicum

substrate_name: dopamine

sequence_source: UniProtKB direct accession lookup A0A3P3ZKL1 via rest.uniprot.org/uniprotkb/A0A3P3ZKL1.json on 2026-06-05

substrate: dopamine


organism: Unknown


organism: Mycothermus thermophilus

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_M4GGR7_and_PMID_30289408_I314F and applied mutation signature I314F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 333.15 K; buffer 100 mM sodium phosphate


organism: Pouteria sapota

substrate_name: pyrogallol

proof_lines: isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C

substrate: pyrogallol


organism: Agaricus bisporus

proof_lines:
pH 7.0
pH 4.5, dependent on the assay method
pH 6.0


organism: Alternaria alternata

substrate_name: D-catechin

substrate: D-catechin


organism: Amphioctopus fangsiao

assay_conditions_summary: pH 7.1; 301.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer at pH 7.1 and 28°C


organism: Anethum foeniculum

proof_lines: at pH 6.0 and 30°C, with catechol as substrate


organism: Aphonopelma californicum (nom. dub.)

proof_lines: at substrate concentrations above 4 mM, substrate inhibition is observed and the data are fitted to a simple model for substrate inhibition. KM, kcat and KI are obtained for the inhibitory binding site


organism: Asimina triloba

proof_lines: Km of pawpaw fruit PPO is comparable with the Km of PPO from other fruits


smiles: OO


organism: Prunus armeniaca

proof_lines: kcat is 700 sec(-1) with 4-methylcatechol as substrate. kcat is 1400 sec(-1) with chlorogenic acid as substrate. kcat is 210 sec(-1) with catechol as substrate. kcat is 590 sec(-1) with pyrogallol as substrate.


organism: Cydonia oblonga


organism: Cynara cardunculus var. scolymus


organism: Erimacrus isenbeckii

proof_lines: at 22°C, pH not specified in the publication


organism: Eriobotrya japonica

substrate_name: tert-butyl-catechol

proof_lines: pH 4.5, 25°C, soluble, active enzyme form

proof_lines: pH 4.5, 25°C, particulate, latent enzyme form

substrate: tert-butyl-catechol


organism: Ferula sp.

substrate_name: (+)-catechin

proof_lines:
pH 6.5, 30°C, stem enzyme
pH 6.0, 20°C, stem enzyme
pH 7.0, 12°C, stem enzyme

substrate: (+)-catechin


organism: Fragaria x ananassa


organism: Beta vulgaris

proof_lines: pH 6.0, 25°C, soluble enzyme in presence of SDS

proof_lines: pH 6.0, 25°C, membrane enzyme in presence of SDS


organism: Bos taurus


organism: Citrus unshiu


organism: Clonorchis sinensis


organism: Coffea arabica

proof_lines:
leaf enzyme
endosperm enzyme


organism: Cucumis melo

substrate_name: 3,4-dihydroxyphenylacetic acid

proof_lines: for Cucumis melo L. inodorus cv. Amarillo

proof_lines: for Cucumis melo L. cantalupensis cv. Charentais

substrate: 3,4-dihydroxyphenylacetic acid


organism: Lycopus europaeus


organism: Malus domestica

proof_lines:
isoform mPPO, at pH 6.8 and 25°C
isoform sPPO, at pH 6.8 and 25°C


organism: Musa acuminata


organism: Musa x paradisiaca


organism: Mycelia sterilia


organism: Neurospora crassa


organism: Nicotiana tabacum


organism: Ocimum basilicum


organism: Panulirus argus


organism: Physalis peruviana


organism: Pycnoporus coccineus

substrate_name: O2; Catechol

substrate: O2; Catechol


organism: Raphanus sativus


organism: Vigna unguiculata


organism: Zea mays


organism: Capra capra


organism: Cereibacter sphaeroides


organism: Escherichia coli


organism: Sarcophaga bullata


organism: Scyllarides latus


organism: Streptomyces cyaneofuscatus


organism: Streptomyces glaucescens

substrate_name: 3,4-Dihydroxyphenyl acetic acid

substrate: 3,4-Dihydroxyphenyl acetic acid


organism: Urtica dioica


organism: Kloeckera sp.

proof_lines:
catalase activity
peroxidase activity


organism: Komagataella pastoris


organism: Mycobacterium sp.

substrate_name: o-Dianisidine

proof_lines:
peroxidase activity, pH 4.5, 30°C
catalase activity, pH 7.0, 30°C

substrate: o-Dianisidine


organism: Neurospora crassa


organism: Lablab purpureus


organism: Lactarius salmonicolor


organism: Lilium brownii var. viridulum

substrate_name: gallic acid

proof_lines:
at pH 4.0 and 25°C
at pH 7.0 and 25°C

substrate: gallic acid


organism: Lilium davidii var. unicolor


organism: Lilium lancifolium


organism: Lonicera japonica


organism: Oceanobacillus oncorhynchi

assay_conditions_summary: pH 9; 303.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer (pH 9.0), at 30°C


organism: Pseudomonas aeruginosa


organism: Pseudomonas syringae


organism: Pteris ensiformis

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0)


organism: Rhodospirillum rubrum


organism: Saccharomyces cerevisiae


organism: Serratia marcescens


organism: Talaromyces piceae

proof_lines: catalase from Penicillium piceum strain F-648 at the minimum degree of association (0.3 nM)


organism: Thermoascus aurantiacus


organism: Thermus brockianus


organism: Escherichia coli


organism: Gluconobacter oxydans

proof_lines: pH and temperature not specified in the publication


organism: Haloarcula marismortui


organism: Halobacterium salinarum

proof_lines:
peroxidase activity
catalase activity


organism: Helicobacter pylori


organism: Cyberlindnera mrakii

sequence_source: UniProtKB reviewed Q12723 FASTA fetched by direct EC+organism lookup.

proof_lines:
anionic
anionic form of substrate
neutral form of substrate


organism: Cyberlindnera saturnus

substrate_name: propionate 3-nitronate

proof_lines:
at pH 7.5 and 30°C
pH 8, 30°C
pH 5.5, 30°C

substrate: propionate 3-nitronate


organism: Fusarium oxysporum

substrate_name: nitroethane

assay_conditions_summary: pH 7; 303.15 K; cofactor FAD

substrate: nitroethane


organism: Metarhizium brunneum


organism: Neurospora crassa

substrate_name: ethylnitronate

sequence_source: UniProtKB reviewed Q01284 FASTA fetched by direct EC+organism lookup.

proof_lines: 30°C, pH 8, wild-type enzyme, ethylnitronate as a substrate

substrate: ethylnitronate


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed Q01284 after direct residue check. and applied mutation signature H196N to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 8, mutant enzyme H196N, ethylnitronate as a substrate


organism: Hordeum vulgare

substrate_name: feruloyl-CoA

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

substrate: feruloyl-CoA


organism: Humulus lupulus

substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


organism: Hypericum androsaemum

substrate_name: benzoyl-CoA

substrate: benzoyl-CoA


proof_lines: pH 7.0, 35°C, mutant enzyme L263M/F265Y/S338G


organism: Juglans sp.

substrate_name: malonyl-CoA

substrate: malonyl-CoA


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 7.2; 303.15 K; cofactor CoA

proof_lines:
isoform CHS8, at pH 7.2 and 30°C
isoform CHS24, at pH 7.2 and 30°C


organism: Petroselinum crispum

substrate_name: hexanoyl-CoA

sequence_source: UniProtKB P16107 FASTA retrieved by direct EC+organism lookup

assay_conditions_summary: cofactor CoA

substrate: hexanoyl-CoA


organism: Phaseolus vulgaris


organism: Scutellaria baicalensis

substrate_name: Malonyl-CoA; Cinnamoyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: Malonyl-CoA; Cinnamoyl-CoA


organism: Secale cereale

substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


organism: Sinapis alba


organism: Styphnolobium japonicum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


organism: Tulipa hybrid cultivar


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Trichoderma viride

enzyme: glucan 1,3-beta-glucosidase


organism: Verruciconidia persicina

substrate_name: Laminarin

proof_lines: enzyme I, based on molecular mass for laminarin of 5300

proof_lines: enzyme II, based on molecular mass for laminarin of 5300

proof_lines: enzyme IIII, based on molecular mass for laminarin of 5300

substrate: Laminarin


enzyme_display_name: licheninase

organism: Acetivibrio thermocellus

assay_conditions_summary: pH 7; 310.15 K; buffer pH 7

proof_lines: pH 7.0, 37°C, 50 mM sodium phosphate buffer

enzyme: licheninase


organism: Aspergillus niger

substrate_name: lichenan

substrate: lichenan


organism: Bacillus amyloliquefaciens

substrate_name: AZO blue beta-glucan

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

substrate: AZO blue beta-glucan


proof_lines: recombinant optimally-modified enzyme, pH 6.5, 40°C


organism: Bacillus sp. (in: firmicutes)


proof_lines:
wild type
wild type, mg/ml


enzyme_display_name: phosphate acetyltransferase

organism: Methanosarcina thermophila

substrate_name: CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature S309A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 296.15 K; cofactor CoA

enzyme: phosphate acetyltransferase

substrate: CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature D316E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature S309C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature R310K to reconstruct the assayed variant sequence.


substrate_name: Acetyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature C312A to reconstruct the assayed variant sequence.

smiles: CC(=O)OP(=O)(O)O

substrate: Acetyl phosphate


substrate_name: Acetyl phosphate; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature C159A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C159A

substrate: Acetyl phosphate; Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature C277A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R287Q


organism: Azotobacter vinelandii

substrate_name: acetyl-CoA

sequence_source: UniProtKB C1DQG8 direct REST lookup on 2026-06-05.

assay_conditions_summary: pH 7.2; 308.15 K; cofactor CoA

proof_lines: pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB

substrate: acetyl-CoA


sequence_source: UniProtKB C1DER7 direct REST lookup on 2026-06-05.


organism: Escherichia coli

substrate_name: Coenzyme A; Acetyl phosphate

sequence_source: UniProtKB P0A9M8 direct REST lookup on 2026-06-05.

substrate: Coenzyme A; Acetyl phosphate


sequence_source: UniProtKB P0A9M8 canonical sequence checked on 2026-06-05; row-specific construct sequence unresolved.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant Pta-F1 (last 326 amino acids), N-terminal His-tag

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant Pta-F2 (last 352 amino acids), N-terminal His-tag

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant Pta-F3 (last 470 amino acids), N-terminal His-tag


proof_lines: wild-type, pH 8.0, 30°C, Hill-constatn 1.7

proof_lines: wild-type, pH 8.0, 30°C, S0.5-value, Hill constant 1.3


sequence_source: UniProtKB P38503 direct REST lookup on 2026-06-05.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific R310A substitution reconstructed on 2026-06-05. and applied mutation signature R310A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific S309T substitution reconstructed on 2026-06-05. and applied mutation signature S309T to reconstruct the assayed variant sequence.


enzyme_display_name: Phosphate acetyltransferase

substrate_name: Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature R310Q to reconstruct the assayed variant sequence.

enzyme: Phosphate acetyltransferase

substrate: Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C325A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C325A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C312A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature R133Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R133Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature R28Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R28Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C159S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates.

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 UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature R87Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R87Q


sequence_source: UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature R28Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature R310Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R310Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature C312A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C312A


organism: Escherichia coli (strain K12)

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


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature R133Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature R310Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature C159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature C159A/C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row SABIO-RK PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature C159A/C277A/C312A/C325A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C159A, C277A, C312A, C325A


sequence_source: UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature R287Q to reconstruct the assayed variant sequence.


organism: Neurospora crassa

substrate_name: 3-nitropropionic acid

sequence_source: UniProtKB reviewed accession Q01284 (2NPD_NEUCR), direct EC 1.13.12.16 plus organism Neurospora crassa lookup

assay_conditions_summary: pH 7.4; 303.15 K; cofactor FMN

proof_lines:
at pH 7.4 and 30°C
at pH 9.0 and 30°C
anionic form of substrate

substrate: 3-nitropropionic acid


organism: Antirrhinum majus

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C

proof_lines: in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C


organism: Avena sativa

substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


organism: Daucus carota


organism: Fagopyrum esculentum


organism: Glycine max

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Porphyromonas gingivalis

sequence_source: UniProtKB:B2RK03 direct lookup

assay_conditions_summary: pH 9; 310.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific R287Q reconstruction and applied mutation signature R287Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific C277A reconstruction and applied mutation signature C277A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C277A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific R133Q reconstruction and applied mutation signature R133Q to reconstruct the assayed variant sequence.


organism: Moorella thermoacetica

substrate_name: acetyl phosphate

substrate: acetyl phosphate


assay_conditions_summary: pH 7.6; 328.15 K; cofactor CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


organism: Neomoorella thermoacetica

sequence_source: UniProtKB Q2RK58 canonical sequence


sequence_source: UniProtKB Q2RJ94 canonical sequence


sequence_source: UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence.

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


substrate_name: Coenzyme A; Acetyl phosphate / Acetyl phosphate; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C159S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C159S


substrate_name: Acetyl phosphate; Coenzyme A / Coenzyme A; Acetyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C277A, C312A, C325A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature R28Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C277A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature R87Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C159A to reconstruct the assayed variant sequence.


enzyme_display_name: UMP kinase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D93A/D159N to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

proof_lines: D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP

enzyme: UMP kinase


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature N72A/D93A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH 7.4, 30°C, mutants N72A and N72A/D93A

proof_lines: pH 7.4, 30°C, mutant N72A/D93A, in absence of GTP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature N140A/D159N to reconstruct the assayed variant sequence.

proof_lines: N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP


substrate_name: ATP; UMP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D201N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant D201N

substrate: ATP; UMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D174N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor ATP

proof_lines:
mutant D174N, at pH 6
mutant D174N, at pH 8


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D146N to reconstruct the assayed variant sequence.

proof_lines:
mutant D146N, at pH 6
mutant D146N, at pH 8


substrate_name: UMP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature R62H to reconstruct the assayed variant sequence.

proof_lines:
mutant R62H, at pH 8
mutant R62H, at pH 6

substrate: UMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D168N to reconstruct the assayed variant sequence.

proof_lines:
mutant D168N, at pH 8
mutant D168N, at pH 6


sequence_source: UniProtKB direct accession lookup P0A7E9 on 2026-06-05

assay_conditions_summary: pH 6; 303.15 K; cofactor ATP

proof_lines:
wild-type
wild-type, at pH 6
wild-type, at pH 6.0


substrate_name: UMP; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N140A reconstruction on 2026-06-05 and applied mutation signature N140A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) wildtype N140A His-tagged

substrate: UMP; ATP


sequence_source: UniProtKB direct accession lookup A7ZWB7 on 2026-06-05

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

proof_lines: in presence of 2.0 mM ATP and 0.5 mM GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based D159N reconstruction on 2026-06-05 and applied mutation signature D159N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) wildtype D159N His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N72A/D93A/D159N reconstruction on 2026-06-05 and applied mutation signature N72A/D93A/D159N to reconstruct the assayed variant sequence.

proof_lines: N72A/D93A/D159N mutant protein, 0.3 mM UMP

proof_lines: N72A/D93A/D159N mutant protein, 2 mM ATP

proof_lines: N72A/D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N72A/D159N reconstruction on 2026-06-05 and applied mutation signature N72A/D159N to reconstruct the assayed variant sequence.

proof_lines: N72A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

proof_lines: N72A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N72A reconstruction on 2026-06-05 and applied mutation signature N72A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based D93A reconstruction on 2026-06-05 and applied mutation signature D93A to reconstruct the assayed variant sequence.


organism: Haemophilus influenzae

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

sequence_source: UniProtKB P43890 canonical FASTA retrieved by direct exact accession lookup

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


organism: Helicobacter pylori

source_db: brenda;skid

sequence_source: UniProtKB P56106 canonical FASTA retrieved by direct exact accession lookup

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

proof_lines: in the presence of 2 mM Mg2+, at pH 7.4 and 30°C

proof_lines: in the presence of 2 mM Mn2+, at pH 7.4 and 30°C

source: brenda;skid


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 canonical FASTA; P139A reconstructed from the returned canonical sequence and applied mutation signature P139A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P9WHK5 canonical FASTA retrieved by direct exact accession lookup

proof_lines: Ki above 1 mM, wild type enzyme, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 canonical FASTA; F81W/S96A reconstructed from the returned canonical sequence and applied mutation signature F81W/S96A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F81W/S96A, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 canonical FASTA; D113A reconstructed from the returned canonical sequence and applied mutation signature D113A to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus

sequence_source: UniProtKB Q2FZ22 REST lookup, reviewed Swiss-Prot entry PYRH_STAA8.


sequence_source: UniProtKB B8XPY6 REST lookup, live TrEMBL entry flagged as fragment.

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

proof_lines: crude cytosolic extract, in 50 mM Tris-HCl pH 7.4, at 30°C

proof_lines: purified enzyme, in 50 mM Tris-HCl pH 7.4, at 30°C


organism: Streptococcus pneumoniae

sequence_source: UniProtKB Q97R83 REST lookup, reviewed Swiss-Prot entry PYRH_STRPN.

proof_lines:
in the presence of MnCl2
in the presence of MgCl2


organism: Ureaplasma parvum

sequence_source: UniProtKB Q9PPX6 REST lookup, reviewed Swiss-Prot entry PYRH_UREPA.

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines:
pH 6.8
recombinant UpUMPK
competitive inhibitor towards UMP


enzyme_display_name: pepsin A

organism: Lateolabrax japonicus

substrate_name: hemoglobin

sequence_source: UniProtKB E2IKQ9 REST lookup, live TrEMBL pepsin A entry.

enzyme: pepsin A

substrate: hemoglobin


assay_conditions_summary: pH 3; 310.15 K; buffer sodium acetate

proof_lines: isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C


organism: Micropterus salmoides

substrate_name: KPAEFFRL

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

substrate: KPAEFFRL


sequence_source: UniProtKB A0A125SQG8 REST lookup, live TrEMBL pepsin A entry.

proof_lines:
pepsin A1, at pH 4.0 and 20°C
pepsin A1, at pH 4.0 and 37°C
pepsin A1, at pH 4.0 and 45°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed P139H substitution and applied mutation signature P139H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed P139W substitution and applied mutation signature P139W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed R82H substitution and applied mutation signature R82H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed R150A substitution and applied mutation signature R150A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed F81W substitution and applied mutation signature F81W to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB P9WHK5 direct check

source: skid


organism: Neisseria meningitidis

sequence_source: UniProtKB P65932 direct check

proof_lines: in presence of 0.05 mM UMP and 0.5 mM GTP

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


organism: Saccharolobus solfataricus

sequence_source: UniProtKB Q97ZE2 direct check

assay_conditions_summary: 333.15 K; cofactor ATP

proof_lines: radioactive assay, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature

proof_lines: radioactive assay, 500 microM ATP and 100 microM UMP, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature


sequence_source: UniProtKB A0A125SQG9 direct accession lookup

proof_lines:
pepsin A2, at pH 4.0 and 20°C
pepsin A2, at pH 4.0 and 30°C
pepsin A2, at pH 4.0 and 10°C


organism: Shewanella amazonensis

substrate_name: Mca-KKPAEFFALK-Dnp

sequence_source: UniProtKB A1S3N8 direct accession lookup

substrate: Mca-KKPAEFFALK-Dnp


organism: Shewanella denitrificans

sequence_source: UniProtKB Q12R32 direct accession lookup


organism: Sus scrofa

substrate_name: H2O; Casein

sequence_source: UniProtKB P00791 direct accession lookup

substrate: H2O; Casein


organism: Trematomus bernacchii

sequence_source: UniProtKB Q6HA04 direct accession lookup


sequence_source: UniProtKB Q6HA05 direct accession lookup


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O31749 direct REST lookup on 2026-06-05; variant reconstructed from selected SABIO-RK N137A note and applied mutation signature N137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant N137A His-tagged


sequence_source: UniProtKB reviewed O31749 direct REST lookup on 2026-06-05

proof_lines:
in the presence of GTP
in the absence of GTP
in presence of 2.0 mM ATP without GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O31749 direct REST lookup on 2026-06-05; variant reconstructed from selected SABIO-RK T135A note and applied mutation signature T135A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant T135A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O31749 direct REST lookup on 2026-06-05; variant reconstructed from selected SABIO-RK T135A/N137A note and applied mutation signature T135A/N137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant T135A/N137A His-tagged


organism: Escherichia coli

sequence_source: UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=6


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05; variant reconstructed from selected BRENDA T138A/N140A note and applied mutation signature T138A/N140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05; variant reconstructed from selected BRENDA T138A note and applied mutation signature T138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05; variant reconstructed from selected BRENDA D77N note and applied mutation signature D77N to reconstruct the assayed variant sequence.

proof_lines:
mutant D77N, at pH 6
mutant D77N, at pH 8


organism: Bacillus subtilis (strain 168)

sequence_source: UniProtKB reviewed accession O31749 (PYRH_BACSU), direct lookup

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


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

substrate_name: Apo-[acyl-carrier protein]; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 direct accession lookup; row-specific reconstruction from R14K/K44D and applied mutation signature R14K/K44D to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS R14K, K44D

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

substrate: Apo-[acyl-carrier protein]; Coenzyme A


substrate_name: Coenzyme A; Apo-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 direct accession lookup; row-specific reconstruction from R14A and applied mutation signature R14A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS R14A

substrate: Coenzyme A; Apo-[acyl-carrier protein]


substrate_name: apo-[acyl-carrier protein]

sequence_source: UniProtKB:P39135 direct accession lookup for enzyme context only

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

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant F44M ACP substrate from Leishmania major

substrate: apo-[acyl-carrier protein]


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli mutant M44F ACP substrate


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M ACP substrate from Leishmania major


sequence_source: UniProtKB:P39135 direct accession lookup

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli ACP substrate

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Mycobacterium tuberculosis

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Plasmodium falciparum


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M/Q48E ACP substrate from Leishmania major


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/Q48E ACP substrate from Leishmania major


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 canonical sequence with selected source mutation R14K applied after residue check and applied mutation signature R14K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS R14K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 canonical sequence with selected source mutation K44A applied after residue check and applied mutation signature K44A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS K44A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 canonical sequence with selected source mutation K44D applied after residue check and applied mutation signature K44D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS K44D


sequence_source: UniProtKB:P96618 direct accession lookup


sequence_source: UniProtKB:P39135 canonical lookup only; row-specific N35D variant sequence unresolved

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D ACP substrate from Leishmania major


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, wild-type ACP substrate from Leishmania major


substrate_name: butyryl-CoA

sequence_source: UniProtKB:P24224 direct accession lookup

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

proof_lines:
pH 7.5, 22°C
Raw SKiD Env: Temp=22°C, pH=7.5

substrate: butyryl-CoA


organism: Homo sapiens

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

sequence_source: UniProtKB:Q9NRN7 direct accession lookup

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


substrate_name: acetyl-CoA / Mg2+

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

proof_lines:
double mutant Q112E, E181Q
+/-0.001 mM, double mutant Q112E, E181Q
+/-51 mM, double mutant Q112E, E181Q

substrate: acetyl-CoA / Mg2+


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed E181A variant and applied mutation signature E181A to reconstruct the assayed variant sequence.


substrate_name: Acetyl-CoA; Apo-[acyl-carrier protein] plus Mg2+/acetyl-CoA source notes

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed H111A variant and applied mutation signature H111A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site H111A


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

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site R47A

substrate: Acetyl-CoA; Apo-[acyl-carrier protein] plus Mg2+/acetyl-CoA source notes


substrate_name: Acetyl-CoA; Apo-[acyl-carrier protein] / Apo-[acyl-carrier protein]; Acetyl-CoA plus Mg2+/acetyl-CoA source notes

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

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site R86A


sequence_source: UniProtKB Q9NRN7 canonical sequence with reconstructed E181A variant

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site E181A

substrate: Acetyl-CoA; Apo-[acyl-carrier protein] / Apo-[acyl-carrier protein]; Acetyl-CoA plus Mg2+/acetyl-CoA source notes


substrate_name: Apo-[acyl-carrier protein]; Acetyl-CoA / Acetyl-CoA; Apo-[acyl-carrier protein] plus Mg2+/acetyl-CoA source notes

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed D129A variant and applied mutation signature D129A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site D129A


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB P50113 canonical sequence


substrate_name: Coenzyme A

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

assay_conditions_summary: pH 5.5; 310.15 K; cofactor CoA

substrate: Coenzyme A


organism: Streptomyces griseus

substrate_name: apo-[fredericamycin H acyl-carrier protein]

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


organism: Streptomyces verticillus

substrate_name: apo-[peptidyl carrier protein]

proof_lines:
pH 8.0, 37°C, substrate BlmI
pH 8.0, 37°C, substrate TcmM
pH 8.0, 37°C

substrate: apo-[peptidyl carrier protein]


organism: Vibrio harveyi

substrate_name: apo-acyl-carrier protein

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

proof_lines: pH 7.8, 37°C, mutant acyl carrier protein I54L

substrate: apo-acyl-carrier protein


proof_lines: pH 7.8, 37°C, Escherichia coli acyl carrier protein


proof_lines: pH 7.8, 37°C, mutant acyl carrier protein Y71A


proof_lines: pH 7.8, 37°C, mutant acyl carrier protein V12G


substrate_name: apo-ACP

proof_lines: pH 7.8, 37°C, mutant acyl carrier protein F50A

substrate: apo-ACP


substrate_name: GDSLSWLLRCLN

assay_conditions_summary: pH 8.8; 310.15 K; cofactor CoA

proof_lines:
pH 8.8, 37°C, isoenzyme Sfp
pH 8.8, 37°C, isoenzyme Sfp, apo-hPCP
pH 6.0, 37°C

substrate: GDSLSWLLRCLN


organism: Unknown


proof_lines: pH 7.8, 37°C, mutant acyl carrier protein A59G


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: CoA

substrate: CoA


organism: Escherichia coli (strain K12)

substrate_name: acetyl phosphate

proof_lines: kcat is 415.5 sec(-1) for acetyl-CoA formation, kcat is 119.8 sec(-1) for acetyl phosphate formation.

substrate: acetyl phosphate


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


substrate_name: 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

substrate: ATP


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

substrate_name: Unknown

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

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


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)


substrate_name: magnesium

substrate: magnesium


enzyme_display_name: indole-3-glycerol-phosphate synthase

organism: Bacillus subtilis

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)


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

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

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.


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


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: 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 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.


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


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.


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


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


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


organism: Saccharomyces cerevisiae

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


organism: Homo sapiens

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.


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.


substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


organism: Chlorogonium elongatum


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: CoA

substrate: 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


organism: Thermus thermophilus


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


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