sequence_variant_note: Resolved canonical sequence from UniProtKB O55137 live lookup plus selected SABIO-RK H358Q modifier note; residue 358 in canonical O55137 is H and was substituted to Q. and applied mutation signature H358Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H358Q His-tagged


enzyme_display_name: palmitoyl-CoA hydrolase

organism: Mus musculus

substrate_name: H2O; Palmitoyl-CoA

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB O55137 live lookup plus selected SABIO-RK S232C modifier note; residue 232 in canonical O55137 is S and was substituted to C. and applied mutation signature S232C to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant S232C His-tagged

enzyme: palmitoyl-CoA hydrolase

substrate: H2O; Palmitoyl-CoA


substrate_name: H2O; Hexanoyl-CoA

mutation_signature: Unknown

sequence_source: UniProtKB Q6Q2Z6 live lookup; source SABIO-RK records cite Q6Q2Z6 for Mus musculus PMID 15007068.

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

substrate: H2O; Hexanoyl-CoA


substrate_name: Hexanoyl-CoA; H2O

sequence_source: UniProtKB Q9QYR7 live lookup; source SABIO-RK records cite Q9QYR7 for Mus musculus PMID 15007068.

substrate: Hexanoyl-CoA; H2O


sequence_source: UniProtKB Q91V12 live lookup; source SABIO-RK records cite Q91V12 for Mus musculus PMID 15288813.


substrate_name: palmitoyl-CoA

source_db: brenda

source_license: CC BY 4.0

sequence_source: UniProtKB Q9QYR9 live lookup; selected BRENDA snapshots cite Q9QYR9 for Mus musculus palmitoyl-CoA and myristoyl-CoA rows.

assay_conditions_summary: pH 7.6; 310.15 K; cofactor CoA

substrate: palmitoyl-CoA

source: brenda


organism: Mycobacterium tuberculosis

substrate_name: dodecanoyl-CoA

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

sequence_source: UniProtKB P9WM67 live lookup; selected BRENDA/SKiD snapshots cite P9WM67 for Mycobacterium tuberculosis substrate rows.

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines:
pH 7.5
Raw SKiD Env: Temp=-----, pH=7.5

source_databases_merged: brenda skid

substrate: dodecanoyl-CoA


organism: Homo sapiens

source_db: uniprot

source: uniprot


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


substrate_name: taurine toward choloyl-CoA

substrate: taurine toward choloyl-CoA


substrate_name: palmitoyl-CoA (C16:0)

substrate: palmitoyl-CoA (C16:0)


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: Arachidonoyl-CoA

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines:
isozyme MTE-I, pH 7.4, 37°C
isozyme CTE-I, pH 7.4, 37°C

substrate: Arachidonoyl-CoA


substrate_name: hexanoyl-coA

substrate: hexanoyl-coA


substrate_name: palmitoyl-CoA (isoform A at 30 degrees Celsius)


substrate_name: propanoyl-CoA

substrate: propanoyl-CoA


organism: Escherichia coli (strain K12)

proof_lines: kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as


substrate_name: n-decanoyl-CoA

proof_lines: kcat is 0.016 sec(-1) for n-decanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.0047 sec(-1) for n-octanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.022 sec(-1) for n-hexanoyl-CoA hydrolase activity (PubMed:19170545). kc

substrate: n-decanoyl-CoA


substrate_name: Unknown

km_display: Not reported

proof_lines: kcat is 5 min(-1) for the hydrolysis of hexadecanoyl-CoA (PubMed:22897136). kcat is 3.5 min(-1) for the hydrolysis of tetradecanoyl-CoA (PubMed:22897136). kcat is 2.3 min(-1) for the hydrolysis of dodecanoyl-CoA (PubMed:22897136). kcat is 0

substrate: Unknown


substrate_name: acetoacetyl-CoA

proof_lines: kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1) for octanoyl-CoA hydrolysis (PubMed:254

substrate: acetoacetyl-CoA


substrate_name: acetyl-CoA

proof_lines: In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 uM, and with short-chain acyl CoAs range from 8 to 30 uM. KM for bile acid-CoA esters is in the range 6-15 uM.

substrate: acetyl-CoA


substrate_name: hexanoyl-CoA (at 37 degrees Celsius)

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

proof_lines: kcat is 3 sec(-1) for hexanoyl-CoA hydrolase activity (at 37 degrees Celsius) (PubMed:19405909). kcat is 5 sec(-1) for decanoyl-CoA hydrolase activity (at 37 degrees Celsius) (PubMed:19405909). kcat is 3 sec(-1) for dodecanoyl-CoA hydrolase

substrate: hexanoyl-CoA (at 37 degrees Celsius)


organism: Rattus norvegicus


data_origin: experimental


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.037 sec(-1) with palmitoyl-CoA as substrate. kcat is 0.019 sec(-1) with stearoyl-CoA as substrate. kcat is 0.015 sec(-1) with lauroyl-CoA as substrate. kcat is 0.012 sec(-1) with hexanoyl-CoA as substrate.


proof_lines: kcat is 0.00342 sec(-1) with palmitoyl-CoA as substrate.


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: p-nitrophenyl butyrate

verification_status: unverified

proof_lines: The N-terminal esterase domain, when expressed alone, shows activities five to ten times higher than those of the complete enzyme EstP towards all tested substrates, whereas substrate affinity and the activity profiles are still the same.

substrate: p-nitrophenyl butyrate

status: unverified


organism: Arabidopsis thaliana

sequence_source: UniProtKB:F4HU51; PMID 14660652

assay_conditions_summary: pH 8; cofactor CoA


organism: Bos taurus


organism: Buckleyzyma aurantiaca

substrate_name: stearoyl-CoA

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

substrate: stearoyl-CoA


organism: Cavia porcellus

substrate_name: hexadecanoyl-CoA

substrate: hexadecanoyl-CoA


organism: Cereibacter sphaeroides

assay_conditions_summary: pH 7.8; 295.15 K; cofactor CoA


organism: Cricetulus griseus

substrate_name: H2O; Palmitoyl-CoA

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

substrate: H2O; Palmitoyl-CoA


organism: Diutina rugosa

substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


organism: Escherichia coli

substrate_name: fatty-acyl-CoA thioester

substrate: fatty-acyl-CoA thioester


organism: Euglena gracilis

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


organism: Mougeotia scalaris


organism: Mycolicibacterium smegmatis


substrate_name: oleoyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines:
pH 7.5, 37°C
for the microsomal enzyme

substrate: oleoyl-CoA


substrate_name: H2O; Myristoyl-CoA

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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant delta39 C-terminal His6-tag

substrate: H2O; Myristoyl-CoA


substrate_name: myristoyl-CoA

source_db: oed

kcat_over_km_origin: calculated

sequence_source: UniProtKB reviewed entry Q5T1C6 / THEM4_HUMAN FASTA, checked directly during review.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: myristoyl-CoA

source: oed


substrate_name: Linoleoyl-CoA

verification_status: corrected

sequence_source: UniProtKB reviewed entry Q8N1Q8 / THEM5_HUMAN FASTA, checked directly during review.

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:2`: Km (uM) = 4.2; kcat (s^-1) = 12.2; kcat/Km (M^-1 s^-1) = 2.9x10^6.

normalized_value_unit_evidence: kcat: printed cell 12.2 s^-1 -> 12.2 s^(-1) (already per second, carried unchanged); the exported value is 12.2 s^(-1). Km: printed cell 4.2 uM -> 0.0042 mM (divide by 1000); the exported value is 0.004 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.9x10^6 M^-1 s^-1 for this substrate line -> 2900.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 3049.9999999999995 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:2`

table_label: Figure 2F (PDF page 5 of 13, journal page 2689) 'Steady-state kinetic constants for hThem5 catalyzed hydrolysis of selected Acyl-CoA esters'

substrate: Linoleoyl-CoA

status: corrected


substrate_name: Palmitoleoyl-CoA

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C16:1`: Km (uM) = 26.7; kcat (s^-1) = 11.5; kcat/Km (M^-1 s^-1) = 4.3x10^5.

normalized_value_unit_evidence: kcat: printed cell 11.5 s^-1 -> 11.5 s^(-1) (already per second, carried unchanged); the exported value is 11.5 s^(-1). Km: printed cell 26.7 uM -> 0.0267 mM (divide by 1000); the exported value is 0.027 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.3x10^5 M^-1 s^-1 for this substrate line -> 430.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 425.9259259259259 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C16:1`

substrate: Palmitoleoyl-CoA


substrate_name: Oleoyl-CoA

substrate: Oleoyl-CoA


sequence_variant_note: Resolved canonical sequence from PMID 22586271 Materials and Methods sequence for human THEM5 35-247 with C-terminal His6 tag. and applied mutation signature Δ34 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) wildtype delta34Them5


column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:0`: Km (uM) = 4.2; kcat (s^-1) = 1.2; kcat/Km (M^-1 s^-1) = 2.9 x10^5.

normalized_value_unit_evidence: kcat: printed cell 1.2 s^-1 -> 1.2 s^(-1) (already per second, carried unchanged); the exported value is 1.2 s^(-1). Km: printed cell 4.2 uM -> 0.0042 mM (divide by 1000); the exported value is 0.004 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.9 x10^5 M^-1 s^-1 for this substrate line -> 290.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 300.0 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:0`


substrate_name: alpha-Linolenoyl-CoA

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:3`: Km (uM) = 15.4; kcat (s^-1) = 13.3; kcat/Km (M^-1 s^-1) = 8.6x10^5.

normalized_value_unit_evidence: kcat: printed cell 13.3 s^-1 -> 13.3 s^(-1) (already per second, carried unchanged); the exported value is 13.3 s^(-1). Km: printed cell 15.4 uM -> 0.0154 mM (divide by 1000); the exported value is 0.015 mM. kcat/Km: the paper PRINTS the kcat/Km cell 8.6x10^5 M^-1 s^-1 for this substrate line -> 860.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 886.6666666666667 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:3`

substrate: alpha-Linolenoyl-CoA


organism: Rhodotorula aurantiaca

substrate_name: H2O; Octanoyl-CoA

substrate: H2O; Octanoyl-CoA


organism: Sus scrofa

assay_conditions_summary: pH 8; 301.15 K; cofactor CoA

proof_lines: pH 8.0, 28°C, with palmitoyl-CoA as substrate


enzyme_display_name: phosphoenolpyruvate carboxykinase (ATP)

substrate_name: oxaloacetate

sequence_source: UniProtKB P22259 canonical FASTA; R65Q reconstructed after confirming canonical residue 65 is R

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

enzyme: phosphoenolpyruvate carboxykinase (ATP)

substrate: oxaloacetate


sequence_source: UniProtKB P22259 canonical FASTA; H232Q reconstructed after confirming canonical residue 232 is H


sequence_source: UniProtKB P22259 canonical FASTA; K212S reconstructed after confirming canonical residue 212 is K


sequence_source: UniProtKB P22259 canonical FASTA; K254S reconstructed after confirming canonical residue 254 is K


sequence_source: UniProtKB P22259 canonical FASTA from direct REST lookup


sequence_source: UniProtKB P22259 canonical FASTA; S250A reconstructed after confirming canonical residue 250 is S

sequence_variant_note: Mutation signature S250A matches the mutant residue at offset +0 and the reference residue at offset +8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P22259 canonical FASTA; R333Q reconstructed after confirming canonical residue 333 is R


substrate_name: ATP; Oxaloacetate

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

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
at pH 7.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: sabio_rk brenda skid

substrate: ATP; Oxaloacetate


organism: Anaerobiospirillum succiniciproducens

substrate_name: ADP; CO2; Phosphoenolpyruvate

sequence_source: UniProtKB accession O09460 direct REST check

assay_conditions_summary: cofactor ATP

substrate: ADP; CO2; Phosphoenolpyruvate


substrate_name: CO2; ADP; Phosphoenolpyruvate

sequence_source: UniProtKB accession O09460 canonical sequence with T249A substitution applied after residue check

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant Thr249Ala

substrate: CO2; ADP; Phosphoenolpyruvate


substrate_name: Phosphoenolpyruvate; CO2; ADP

sequence_source: UniProtKB accession O09460 canonical sequence with D262E substitution applied after residue check

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant Asp262Glu

substrate: Phosphoenolpyruvate; CO2; ADP


sequence_source: UniProtKB accession Q9T074 direct REST check

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


substrate_name: ADP

sequence_source: UniProtKB accession B5X574 direct REST check

substrate: ADP


substrate_name: phosphoenolpyruvate

sequence_source: UniProtKB accession P22259 direct REST check

substrate: phosphoenolpyruvate


sequence_source: UniProtKB accession P22259 canonical sequence with K213S substitution applied after residue check


sequence_source: UniProtKB accession P22259 canonical sequence with D269N substitution applied after residue check


organism: Leishmania major

sequence_source: UniProtKB REST accession E9ADF9

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession E9ADF9 and applied mutation signature Y180F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession E9ADF9 and applied mutation signature H205Q to reconstruct the assayed variant sequence.


substrate_name: ADP; phosphoenolpyruvate; ATP; oxaloacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession E9ADF9 and applied mutation signature Y180A to reconstruct the assayed variant sequence.


organism: Ruminococcus albus

substrate_name: ADP; phosphoenolpyruvate; oxaloacetate; ATP

sequence_source: UniProtKB REST accession B3Y6D3

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

assay_conditions_summary: pH 7; cofactor ATP


organism: Saccharomyces cerevisiae

substrate_name: Phosphoenolpyruvate; CO2; ADP; ADP; CO2; Phosphoenolpyruvate; Phosphoenolpyruvate; ADP; CO2

sequence_source: UniProtKB REST accession P10963

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P10963 and applied mutation signature R336Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant R336Q


substrate_name: ADP; Phosphoenolpyruvate; CO2; ADP; CO2; Phosphoenolpyruvate; CO2; ADP; Phosphoenolpyruvate; Oxaloacetate; ATP

proof_lines:
ADP in form of MnADP-
CO2 in form of HCO3-
ATP in form of MnATP2-


substrate_name: CO2; Phosphoenolpyruvate; ADP; Phosphoenolpyruvate; CO2; ADP; CO2; ADP; Phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P10963 and applied mutation signature R336K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant R336K


organism: Trypanosoma cruzi

ki_unit: mM

sequence_source: UniProtKB reviewed accession P51058

assay_conditions_summary: pH 9; cofactor ATP


organism: Unknown


substrate_name: ADP (at 37 degrees Celsius and at pH 6.2)


organism: Escherichia coli (strain K12)

substrate_name: manganese (at 31 degrees Celsius and pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying Y180A to the canonical E9ADF9 sequence; canonical residue 180 was Y. and applied mutation signature Y180A to reconstruct the assayed variant sequence.


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying Y180F to the canonical E9ADF9 sequence; canonical residue 180 was Y. and applied mutation signature Y180F to reconstruct the assayed variant sequence.

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying H205Q to the canonical E9ADF9 sequence; canonical residue 205 was H. and applied mutation signature H205Q to reconstruct the assayed variant sequence.


sequence_source: UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying Y180F to the canonical E9ADF9 sequence; canonical residue 180 was Y.


sequence_source: UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying H205Q to the canonical E9ADF9 sequence; canonical residue 205 was H.


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


sequence_source: UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Canonical wild-type sequence used unchanged.


substrate_name: IDP

sequence_source: UniProtKB P10963 canonical sequence

assay_conditions_summary: pH 6.9; 303.15 K; cofactor ATP

substrate: IDP


substrate_name: ITP

substrate: ITP


substrate_name: UDP

substrate: UDP


substrate_name: CTP

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P10963 canonical sequence with reviewed T463A substitution reconstructed during review and applied mutation signature T463A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant T463A


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


sequence_source: UniProtKB P10963 canonical sequence with reviewed T463A substitution reconstructed during review


substrate_name: GTP

substrate: GTP


organism: Alternanthera ficoidea

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

proof_lines:
pH 7.3, 37°C, 10 mM bicarbonate
pH 7.3, 37°C, 0.05 mM bicarbonate


organism: Alternanthera ficoides

proof_lines:
pH 7.3, 37°C, 0.05 mM bicarbonate
pH 7.3, 37°C, 10 mM bicarbonate


organism: Alternanthera pungens


organism: Alternanthera sessilis


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09460 plus PMID 14987800 H225E mutation evidence and applied mutation signature H225E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


substrate_name: oxaloacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 272 is E in the canonical 549 aa sequence. and applied mutation signature E272Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.6; 303.15 K; buffer 100 mM MOPS; cofactor ATP

proof_lines: mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 212 is K in the canonical 549 aa sequence. and applied mutation signature K212R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 213 is K in the canonical 549 aa sequence. and applied mutation signature K213Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 460 is L in the canonical 549 aa sequence. and applied mutation signature L460A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM MOPS; cofactor ATP

proof_lines: mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C

proof_lines: mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 299 is E in the canonical 549 aa sequence. and applied mutation signature E299A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C

proof_lines: mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 207 is Y in the canonical 549 aa sequence. and applied mutation signature Y207L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C


organism: Salinivibrio costicola

substrate_name: Unknown

substrate: Unknown


organism: Thermus thermophilus


organism: Trypanosoma brucei


proof_lines:
ATP in form of MnATP2-
ADP in form of MnADP-
CO2 in form of HCO3-


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


proof_lines: condition: 0.1 mM Mn2+, 5 mM Mg2 /Vmax: 37 micromol/min/mg

proof_lines: condition: 4 mM Mn2+ /Vmax: 47 micromol/min/mg


organism: Escherichia coli

substrate_name: ADP

proof_lines:
in presence of Mg2+
CO2 in form of HCO3-
in presence of Mn2+


organism: Megathyrsus maximus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


assay_conditions_summary: pH 6.6; 303.15 K; cofactor ADP


sequence_source: UniProt REST P10963 canonical sequence checked directly during review


sequence_variant_note: Resolved canonical sequence from UniProt REST P10963 canonical sequence with T463A reconstructed during review and applied mutation signature T463A to reconstruct the assayed variant sequence.


substrate_name: GDP

substrate: GDP


sequence_source: UniProt REST P10963 canonical sequence with T463A reconstructed during review


substrate_name: phosphoenolpyruvate

sequence_source: UniProt REST P10963 direct lookup

proof_lines: for the pyruvate kinase-like activity of wild-type

proof_lines: wild-type, apparent kinetic parameters for wild-type in the phosphoenolpyruvate formation direction


sequence_variant_note: Resolved canonical sequence from UniProt REST P10963 direct lookup with R457M reconstruction and applied mutation signature R457M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P10963 direct lookup with S252A reconstruction and applied mutation signature S252A to reconstruct the assayed variant sequence.

proof_lines: S252A mutant, apparent kinetic parameters for S252A mutant in the phosphoenolpyruvate carboxylation direction

proof_lines: for the pyruvate kinase-like activity of S252A mutant

proof_lines: for the oxaloacetate decarboxylase activity of S252A mutant


organism: Selenomonas ruminantium

sequence_source: UniProt REST O83023 direct lookup

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


verification_status: verified

sequence_variant_note: Resolved canonical sequence from UniProtKB:E9ADF9 FASTA direct lookup; Y180A reconstructed from the canonical sequence. and applied mutation signature Y180A to reconstruct the assayed variant sequence.

status: verified


sequence_source: UniProtKB:E9ADF9 FASTA direct lookup.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9ADF9 FASTA direct lookup; H205Q reconstructed from the canonical sequence. and applied mutation signature H205Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9ADF9 FASTA direct lookup; Y180F reconstructed from the canonical sequence. and applied mutation signature Y180F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:E9ADF9 FASTA direct lookup; Y180A reconstructed from the canonical sequence.


sequence_source: UniProtKB:E9ADF9 FASTA direct lookup; H205Q reconstructed from the canonical sequence.


enzyme_display_name: adenosine deaminase

organism: Mus musculus

substrate_name: H2O; Adenosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P03958; reconstructed_variant_sequence:E217Q and applied mutation signature E217Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant E217Q

enzyme: adenosine deaminase

substrate: H2O; Adenosine


substrate_name: Adenosine; H2O

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

substrate: Adenosine; H2O


substrate_name: Adenosine

substrate: Adenosine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P03958; reconstructed_variant_sequence:E217G and applied mutation signature E217G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P03958; reconstructed_variant_sequence:E217D and applied mutation signature E217D to reconstruct the assayed variant sequence.


organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8IJA9; reconstructed_variant_sequence:D176A and applied mutation signature D176A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant D176A

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8IJA9; reconstructed_variant_sequence:C27Q/L227I and applied mutation signature C27Q/L227I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant C27Q+L227I

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I


organism: Bos taurus

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

proof_lines:
kidney cortex large isozyme
spleen small isozyme
lung small isozyme


organism: Homo sapiens

substrate_name: adenosine

proof_lines: 25°C, 50 mM Tris-HCl buffer, pH 7.4, enzyme concentration 1.5 nM

substrate: adenosine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8IJA9 canonical sequence; L179H reconstructed after direct residue check confirmed canonical residue 179 is L. and applied mutation signature L179H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant L179H

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme L179H


organism: Schizosaccharomyces pombe

substrate_name: adenine

substrate: adenine


organism: Thermotoga maritima

sequence_source: UniProtKB reviewed accession Q9X034 canonical sequence; retained only as context because the accession EC annotation conflicts with selected EC 3.5.4.4.


organism: Xenopus laevis

sequence_source: UniProtKB reviewed accession Q2VQV9 canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature T174A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant T174A

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme T174A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature T174I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant T174I

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme T174I


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature D176M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant D176M

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176M


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature F136L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant F136L

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme F136L


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature D176A/L179H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant D176A+L179H


sequence_source: UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature D176A/L179A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A


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


substrate_name: L-citrulline

substrate: L-citrulline


organism: Escherichia coli (strain K12)

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


organism: Gallus gallus

sequence: TPLWSLMQDLMM


substrate_name: adenosine (for adenosine phosphorylase activity)


substrate_name: adenosine (at 25 degrees Celsius and pH 5.5)


organism: Lutzomyia longipalpis


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)

proof_lines: kcat is 13000 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 33300 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).


proof_lines: kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).

substrate: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

proof_lines: kcat is 1101 min(-1) and 0.47 min(-1) with adenosine and adenine as substrate, respectively.


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: 5'-deoxyadenosine (at pH 9 and 60 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: kcat is 120000 sec(-1) for 5'-deoxyadenosine deamination. kcat is 160 sec(-1) for S-methyl-5'-thioadenosine deamination. kcat is 1300 sec(-1) for S-adenosyl-L-homocysteine deamination. kcat is 110 sec(-1) for adenosine deamination (at pH 9


organism: Plasmodium berghei (strain Anka)

substrate_name: adenosine (at pH 8)

proof_lines: kcat is 4.7 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.35 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).

substrate: adenosine (at pH 8)


organism: Plasmodium cynomolgi (strain B)

proof_lines: kcat is 5.3 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.31 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


organism: Plasmodium falciparum (isolate 3D7)

proof_lines: kcat is 4.1 sec(-1) with adenosine as substrate (PubMed:31002765). kcat is 5.6 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 13.92 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:31002765). kcat is 5.8 sec(-1) with


organism: Plasmodium gallinaceum

proof_lines: kcat is 1.9 sec(-1) with adenosine as substrate.


organism: Plasmodium knowlesi

proof_lines: kcat is 6.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.51 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


organism: Plasmodium vivax (strain Salvador I)

proof_lines: kcat is 1.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.13 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

proof_lines: kcat is 11.5 sec(-1) with adenosine as substrate.


organism: Unknown prokaryotic organism

proof_lines: kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 660 sec(-1) with syringaldazine as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as substrate (at pH 4.5 and 40 degrees Celsius).


organism: Homo sapiens

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


sequence_variant_note: Resolved canonical sequence from uniprot_canonical_sequence_plus_residue_substitution and applied mutation signature D8N to reconstruct the assayed variant sequence.


proof_lines: pH 7.4, temperature not specified in the publication


organism: Methanocaldococcus jannaschii

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

proof_lines: pH and temperature not specified in the publication, mutant enzyme Y136R


proof_lines: pH and temperature not specified in the publication, wild-type enzyme


proof_lines: pH and temperature not specified in the publication, mutant enzyme E150R


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_canonical_sequence_plus_residue_substitution and applied mutation signature E217G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant E217G


sequence_variant_note: Resolved canonical sequence from uniprot_canonical_sequence_plus_residue_substitution and applied mutation signature E217D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant E217D


organism: Escherichia coli


organism: Fasciola gigantica


organism: Gallus gallus


organism: Hyalomma dromedarii


organism: Kitasatospora aureofaciens


organism: Klebsiella sp.


organism: Argopecten irradians concentricus

substrate_name: 6-Chloropurine riboside

substrate: 6-Chloropurine riboside


organism: Aspergillus terricola


organism: Bacillus cereus


organism: Biomphalaria glabrata


organism: Camelus dromedarius


organism: Danio rerio

proof_lines:
membrane-bound ADA
soluble fraction


organism: Arabidopsis thaliana

sequence_source: UniProtKB direct lookup Q8LPL7

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


organism: Bos taurus

sequence_source: UniProtKB direct lookup P56658

proof_lines: pH 7.0, temperature not specified in the publication


wild_type_sequence: TPLWSLMQDLMM

sequence_source: UniProtKB direct lookup P84520


organism: Helicobacter pylori

sequence_source: UniProtKB direct lookup O25046


organism: Homo sapiens

sequence_source: UniProtKB direct lookup P00813

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

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme, wild-type enzyme (refolded)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup P00813 and applied mutation signature M155A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant M155A refolded

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme M155A (refolded)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup P00813 and applied mutation signature M155D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant M155D refolded


organism: Rattus norvegicus

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


organism: Streptomyces coelicolor

proof_lines: 37°C, pH not specified in the publication


organism: Streptomyces sp.

substrate_name: AMP

substrate: AMP


organism: Sus scrofa


organism: Trichomonas vaginalis

proof_lines: pH 7.5, 37°C, Vmax is 2.61 nmol NH3/min/mg protein


organism: Xenopus laevis


organism: Mus musculus


organism: Nocardioides sp.


organism: Plasmodium berghei

sequence_source: UniProtKB reviewed A0A509ALD0; adenosine deaminase from Plasmodium berghei strain Anka; EC 3.5.4.4 evidence cites PMID 19728741.

assay_conditions_summary: pH 8; buffer 100 mM Tris-HCl

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication


organism: Plasmodium cynomolgi

sequence_source: UniProtKB reviewed K6UCV4; adenosine deaminase from Plasmodium cynomolgi strain B; EC 3.5.4.4 evidence cites PMID 19728741.


organism: Plasmodium falciparum

sequence_source: UniProtKB reviewed Q8IJA9; adenosine deaminase from Plasmodium falciparum isolate 3D7; EC 3.5.4.4 evidence cites PMID 19728741.


organism: Plasmodium gallinaceum

sequence_source: UniProtKB A0A0K1SC59 canonical reviewed entry; EC 3.5.4.4 evidence cites PMID 19728741

column_label: Table 2. Kinetic constants for Plasmodium ADAs with adenosine and 5'-methylthioadenosine (MTA) as substrates, printed column heads Species | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | MTA: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); Table 4. Kinetic and inhibition constants for PvADA-mutants, printed column heads Mutant | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | Coformycin: Ki (nM), Ki* (nM). Table 2, species row P. gallinaceum; adenosine column group; Km cell = 32 uM; kcat cell = 1.9 s^-1; kcat/Km cell = 5.9 x 10^4 M^-1 s^-1. captured primary segment: Table 2, adenosine column group, species row P. gallinaceum: Km 32 uM; kcat 1.9 s^-1; kcat/Km 5.9 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 2 cell 32 uM; 1 uM = 1/1000 mM, so 32 / 1000 = 0.032 mM; the export stores 32.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat: printed Table 2 cell 1.9 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 1.9 s^-1; the export stores 1.9 s^-1, the same value. kcat/Km: printed Table 2 cell 5.9 x 10^4 under the printed unit row M^-1 s^-1, which is 59000.0 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 59000.0 / 1000 = 59.0 s^-1 mM^-1; the export stores 59000.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Table 2, species row P. gallinaceum, adenosine column group: Km = 32 uM; kcat = 1.9 s^-1; kcat/Km = 5.9 x 10^4 under the printed unit row M^-1 s^-1.

row_label: Table 2, species row P. gallinaceum


organism: Plasmodium knowlesi


organism: Plasmodium vivax

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5KE01 and applied mutation signature D172E to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic constants for Plasmodium ADAs with adenosine and 5'-methylthioadenosine (MTA) as substrates, printed column heads Species | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | MTA: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); Table 4. Kinetic and inhibition constants for PvADA-mutants, printed column heads Mutant | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | Coformycin: Ki (nM), Ki* (nM). Table 4, mutant row PvADA-Glu172; adenosine column group; Km cell = 83 uM; kcat cell = 12.9 s^-1; kcat/Km cell = 1.5 x 10^5 M^-1 s^-1. captured primary segment: Table 4, adenosine column group, mutant row PvADA-Glu172: Km 83 uM; kcat 12.9 s^-1; kcat/Km 1.5 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 83 uM; 1 uM = 1/1000 mM, so 83 / 1000 = 0.083 mM; the export stores 83.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat: printed Table 4 cell 12.9 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 12.9 s^-1; the export stores 12.9 s^-1, the same value. kcat/Km: printed Table 4 cell 1.5 x 10^5 under the printed unit row M^-1 s^-1, which is 150000.0 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 150000.0 / 1000 = 150.0 s^-1 mM^-1; the export stores 150000.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Table 4, mutant row PvADA-Glu172, adenosine column group: Km = 83 uM; kcat = 12.9 s^-1; kcat/Km = 1.5 x 10^5 under the printed unit row M^-1 s^-1.

row_label: Table 4, mutant row PvADA-Glu172


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5KE01 and applied mutation signature D172A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM Tris-HCl

column_label: Table 2. Kinetic constants for Plasmodium ADAs with adenosine and 5'-methylthioadenosine (MTA) as substrates, printed column heads Species | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | MTA: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); Table 4. Kinetic and inhibition constants for PvADA-mutants, printed column heads Mutant | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | Coformycin: Ki (nM), Ki* (nM). Table 4, mutant row PvADA-Ala172; adenosine column group; Km cell = 104 uM; kcat cell = 14.0 s^-1; kcat/Km cell = 1.3 x 10^5 M^-1 s^-1. captured primary segment: Table 4, adenosine column group, mutant row PvADA-Ala172: Km 104 uM; kcat 14.0 s^-1; kcat/Km 1.3 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 104 uM; 1 uM = 1/1000 mM, so 104 / 1000 = 0.104 mM; the export stores 104.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat: printed Table 4 cell 14.0 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 14.0 s^-1; the export stores 14.0 s^-1, the same value. kcat/Km: printed Table 4 cell 1.3 x 10^5 under the printed unit row M^-1 s^-1, which is 130000.0 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 130000.0 / 1000 = 130.0 s^-1 mM^-1; the export stores 130000.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Table 4, mutant row PvADA-Ala172, adenosine column group: Km = 104 uM; kcat = 14.0 s^-1; kcat/Km = 1.3 x 10^5 under the printed unit row M^-1 s^-1.

row_label: Table 4, mutant row PvADA-Ala172


assay_conditions_summary: pH 8; 310.15 K; buffer 100 mM Tris-HCl


organism: Plasmodium yoelii


organism: Saccharomyces cerevisiae

substrate: phosphoenolpyruvate


proof_lines: pH high (pH range:6-8.4), pH:12, PEP carboxylation direction

proof_lines: kinetic parameter in the PEP carboxylation direction

substrate: ADP


proof_lines: F216Y: kinetic parameter in the PEP carboxylation direction

proof_lines: F216Y: kinetic parameter in the PEP formation direction


proof_lines: wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C

proof_lines: wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C


assay_conditions_summary: pH 6.6; 303.15 K; buffer 100 mM MOPS

proof_lines: mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C


substrate_name: oxaloacetate

proof_lines: Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C

substrate: oxaloacetate


enzyme_display_name: deoxynucleoside kinase

organism: Drosophila melanogaster

substrate_name: thymidine

enzyme: deoxynucleoside kinase

substrate: thymidine


substrate_name: Thymidine; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence plus selected source mutation signature and applied mutation signature F114Y to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant F114Y

substrate: Thymidine; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence plus selected source mutation signature and applied mutation signature Q81E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9XZT6 canonical sequence


sequence_source: UniProtKB Q9XZT6 canonical sequence plus selected source mutation signature


proof_lines: recombinant N-terminally truncated mutant V84A/M88R, pH 7.6, 37°C

proof_lines: recombinant mutant V84A/M88R, pH 7.6, 37°C


proof_lines: uncompetitive versus 2-deoxythymidine, recombinant mutant N64D

proof_lines: competitive versus ATP, recombinant mutant N64D


proof_lines:
recombinant mutants N45D and N64D
mutant enzyme N45D/N64D


proof_lines:
recombinant mutant N45D
recombinant mutants N45D


proof_lines:
37°C, pH 7.5, mutant enzyme Q81N
pH 7.6, 37°C, recombinant mutant Q81N


organism: Anopheles gambiae

sequence_source: UniProtKB:Q86LB8 direct lookup


organism: Bombyx mori

substrate_name: ATP; Thymidine

sequence_source: UniProtKB:Q9BKL3 direct lookup

substrate: ATP; Thymidine


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature ΔC10 with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant dNKdeltaC10


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature ΔC20 with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant dNKdeltaC20


sequence_source: reconstructed from UniProtKB:Q9XZT6 canonical sequence

sequence_variant_note: Mutation signature ΔC30 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant dNKdeltaC30


sequence_source: UniProtKB:Q9XZT6 direct lookup

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8, 37°C
pH 7.8, 22°C, recombinant enzyme
Raw SKiD Env: Temp=22°C, pH=7.8


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature Q81N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant Q81N


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature F114A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant F114A


proof_lines: recombinant N-terminally truncated mutant M88R, pH 7.6, 37°C


proof_lines: recombinant mutant V84A/M88R/A110D, pH 7.6, 37°C


substrate_name: Dideoxycytidine

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.6, 37°C, recombinant wild-type enzyme

substrate: Dideoxycytidine


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with V84S reconstructed after direct residue check and applied mutation signature V84S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with V84M reconstructed after direct residue check and applied mutation signature V84M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with V84S/M88R/A110D reconstructed after direct residue checks and applied mutation signature V84S/M88R/A110D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with F114Y reconstructed after direct residue check and applied mutation signature F114Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with I29H/Q81D reconstructed after direct residue checks and applied mutation signature I29H/Q81D to reconstruct the assayed variant sequence.

proof_lines: above, pH 7.6, 37°C, recombinant mutants I29H and Q81D


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with F114A reconstructed after direct residue check and applied mutation signature F114A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB direct accession lookup Q9XZT6; reviewed Swiss-Prot entry DNK_DROME, sequence version 1

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


substrate_name: Cytarabine

substrate: Cytarabine


substrate_name: deoxyadenosine

substrate: deoxyadenosine


sequence_source: UniProtKB direct accession lookup Q8UVZ9; live TrEMBL entry Q8UVZ9_XENLA, sequence version 1


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence; reconstructed E52D substitution after direct coordinate check and applied mutation signature E52D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence; reconstructed R105H substitution after direct coordinate check and applied mutation signature R105H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence; reconstructed E52H substitution after direct coordinate check and applied mutation signature E52H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9XZT6 reviewed canonical sequence

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP

proof_lines: 37°C, fusion protein with glutathione S-transferase


enzyme_display_name: 3-dehydroquinate dehydratase

organism: Lancefieldella rimae

sequence_source: UniProtKB REST direct accession lookup for B9CK59 on 2026-06-03

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

enzyme: 3-dehydroquinate dehydratase


organism: Micromonospora lupini

sequence_source: UniProtKB REST direct accession lookup for I0L192 on 2026-06-03


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST direct accession lookup for P9WPX7 on 2026-06-03

proof_lines:
at pH 7.0, 25°C
pH 7, 25°C
recombinant enzyme, pH 7.0, 25°C


organism: Natranaerobius thermophilus

sequence_source: UniProtKB REST direct accession lookup for B2A551 on 2026-06-03


organism: Neurospora crassa

sequence_source: UniProtKB REST direct accession lookup for Q8X071 on 2026-06-03


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB REST direct accession lookup for O30557 on 2026-06-03

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7


organism: Pseudomonas putida

sequence_source: UniProtKB REST direct accession lookup for Q88IJ6 on 2026-06-03


organism: Psychrobacter sp. PRwf-1

sequence_source: UniProtKB REST direct accession lookup for A5WDH9 on 2026-06-03


organism: Streptomyces coelicolor

sequence_source: UniProtKB:P15474 direct accession lookup; reviewed Swiss-Prot entry AROQ_STRCO

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


organism: Thermodesulfobium narugense

sequence_source: UniProtKB:M1E6S9 direct accession lookup; unreviewed TrEMBL entry M1E6S9_9BACT


organism: Thermomonospora curvata

sequence_source: UniProtKB:D1A7X0 direct accession lookup; unreviewed TrEMBL entry D1A7X0_THECD


organism: Xylella fastidiosa

sequence_source: UniProtKB:Q9PH97 direct accession lookup; reviewed Swiss-Prot entry AROQ_XYLFA


organism: Psychromonas ingrahamii

sequence_source: UniProtKB REST FASTA/JSON accession A1SZA3, fetched 2026-06-03


organism: Ruminococcus champanellensis

sequence_source: UniProtKB REST FASTA/JSON accession D4LCT8, fetched 2026-06-03


organism: Salmonella enterica

sequence_source: UniProtKB REST FASTA/JSON accession P58687, fetched 2026-06-03

proof_lines: pH 8.3, temperature not specified in the publication, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P58687 canonical sequence fetched 2026-06-03 by applying K170M and applied mutation signature K170M to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB P58687 canonical sequence fetched 2026-06-03 by applying K170M


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P58687 canonical sequence fetched 2026-06-03 by applying S232A and applied mutation signature S232A to reconstruct the assayed variant sequence.

proof_lines: pH 8.3, temperature not specified in the publication, mutant S232A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P58687 canonical sequence fetched 2026-06-03 by applying Q236A and applied mutation signature Q236A to reconstruct the assayed variant sequence.

proof_lines: pH 8.3, temperature not specified in the publication, mutant Q236A


organism: Streptomyces acidiscabies

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


sequence_variant_note: Resolved canonical sequence from UniProtKB P15474 direct REST lookup; variant reconstructed from PMID 8798709 mutation label. and applied mutation signature R23Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydroquinate dehydratase(Enzyme) mutant R23Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P15474 direct REST lookup; variant reconstructed from PMID 8798709 mutation label. and applied mutation signature R23A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P15474 direct REST lookup; variant reconstructed from PMID 8798709 mutation label. and applied mutation signature R23K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P15474 direct REST lookup; variant reconstructed from PMID 8798709 mutation label.


sequence_source: UniProtKB P15474 direct REST lookup.


proof_lines: SABIO-RK modifier species: 3-dehydroquinate dehydratase(Enzyme) mutant R23A


proof_lines: SABIO-RK modifier species: 3-dehydroquinate dehydratase(Enzyme) mutant R23K


organism: Crystallibacter crystallopoietes

sequence_source: UniProtKB direct lookup: N1V364

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


organism: Enterococcus faecalis

sequence_source: UniProtKB direct lookup: P36923


organism: Escherichia coli

sequence_source: UniProtKB direct lookup: P05194


organism: Eshraghiella crossota

sequence_source: UniProtKB direct lookup: D4S0D1


organism: Halanaerobium hydrogeniformans

sequence_source: UniProtKB direct lookup: E4RLB7


organism: Helicobacter pylori

sequence_source: UniProtKB direct lookup: Q48255

proof_lines:
pH 7.5, 25°C
at pH 7.0, 25°C
in 50 mM Tris-HCl, pH 7, at 25°C


organism: Klebsiella aerogenes

sequence_source: UniProtKB direct lookup: A0A0H3FM50


organism: Arabidopsis thaliana

substrate_name: shikimate

substrate: shikimate


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)


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

substrate_name: quinate

substrate: quinate


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)


sequence_variant_note: Resolved canonical sequence from UniProtKB P58687 canonical sequence with E86Q substitution reconstructed during review and applied mutation signature E86Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P58687 canonical sequence with E86Q substitution reconstructed during review


sequence_variant_note: Resolved canonical sequence from UniProtKB P58687 canonical sequence with E86A substitution reconstructed during review and applied mutation signature E86A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P58687 canonical sequence with E86A substitution reconstructed during review


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB P58687 canonical sequence checked during review

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=8.3

source: skid


organism: Salmonella enterica subsp. enterica serovar Typhi

sequence_source: UniProtKB P24670 canonical sequence checked during review

proof_lines:
pH 7.2, 25°C
Raw SKiD Env: Temp=25°C, pH=7.2


organism: Salmonella typhi


organism: Amycolatopsis methanolica


organism: Aspergillus nidulans


organism: Clostridioides difficile


organism: Eucalyptus camaldulensis

proof_lines:
isoform DQD/SDH3, at pH 7.0 and 30°C
isoform DQD/SDH2, at pH 7.0 and 30°C
isoform DQD/SDH1, at pH 7.0 and 30°C


organism: Geobacillus sp. Y4.1MC1


organism: Acetivibrio clariflavus

sequence_source: UniProtKB:G8M0G7 direct REST lookup on 2026-06-03


organism: Alcanivorax borkumensis

sequence_source: UniProtKB:Q0VMZ2 direct REST lookup on 2026-06-03


organism: Alicyclobacillus acidocaldarius


sequence_source: UniProtKB:P07547 direct REST lookup on 2026-06-03


organism: Bacillus subtilis

sequence_source: UniProtKB:P54517 direct REST lookup on 2026-06-03


organism: Butyrivibrio crossotus

sequence_source: UniProtKB:D4S0D1 direct REST lookup on 2026-06-03


organism: Citrobacter koseri

sequence_source: UniProtKB:A8AQF2 direct REST lookup on 2026-06-03


organism: Corynebacterium glutamicum

sequence_source: UniProtKB:O52377 direct REST lookup on 2026-06-03


organism: Glaciozyma antarctica


organism: Gluconobacter oxydans


organism: Helicobacter pylori


organism: Klebsiella pneumoniae


organism: Lathyrus oleraceus

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


organism: Mycobacterium tuberculosis


proof_lines: mutant enzyme D88N, in Tris/acetic acid (50 mM, pH 8.0) at 25°C


proof_lines: wild type enzyme, in Tris/acetic acid (50 mM, pH 7.0) at 25°C


proof_lines: mutant enzyme N12S, in Tris/acetic acid (50 mM, pH 7.0) at 25°C


organism: Salmonella enterica subsp. enterica serovar Typhi

assay_conditions_summary: pH 7


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: dehydroquinate

substrate: dehydroquinate


organism: Streptomyces coelicolor


organism: Clostridioides difficile (strain 630)

proof_lines: kcat is 125 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius).


organism: Enterococcus faecalis (strain ATCC 700802 / V583)

proof_lines: kcat is 110 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.5 and 25 degrees Celsius).


organism: Escherichia coli (strain K12)

proof_lines: kcat is 142 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7 and 25 degrees Celsius).


organism: Salmonella typhi

proof_lines: kcat is 1.1 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius).


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

proof_lines: kcat is 210 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius). kcat is 255 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius). kcat is 310 sec(-1) for dehydratas


enzyme_display_name: NAD(+) kinase

organism: Euglena gracilis

substrate_name: ATP

assay_conditions_summary: cofactor NAD+

proof_lines:
isoenzyme 1
isoenzyme 2
GTP in form of MgGTP2-

enzyme: NAD(+) kinase

substrate: ATP


organism: Strongylocentrotus purpuratus

substrate_name: NAD+

proof_lines: pH and temperature not specified in the publication

substrate: NAD+


organism: Unknown

substrate_name: Unknown

substrate: Unknown


organism: Methanocaldococcus jannaschii

substrate_name: NAD+; ATP

sequence_source: UniProtKB:Q58327 direct REST check

substrate: NAD+; ATP


assay_conditions_summary: pH 8.5; 358.15 K; cofactor NAD+


assay_conditions_summary: pH 8.5; 358.15 K; cofactor ATP


organism: Micrococcus luteus

sequence_source: UniProtKB:Q8VUL9 direct REST check


substrate_name: ATP; NAD+

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q8VUL9 canonical sequence and selected SABIO-RK G183R mutation note and applied mutation signature G183R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: NAD+ kinase(Enzyme) mutant G183R

substrate: ATP; NAD+


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P9WHV7 canonical sequence and selected SABIO-RK S199A mutation note and applied mutation signature S199A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: NAD+ kinase(Enzyme) mutant S199A


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P9WHV7 canonical sequence and selected SABIO-RK G208A mutation note and applied mutation signature G208A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: NAD+ kinase(Enzyme) mutant G208A


sequence_source: UniProtKB:P9WHV7 direct REST check

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 direct REST lookup, accession P9WHV7, reviewed Swiss-Prot entry NADK_MYCTU and applied mutation signature T195A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: NAD+ kinase(Enzyme) mutant T195A


organism: Pyrococcus horikoshii

sequence_source: UniProtKB direct REST lookup, accession O58801, reviewed Swiss-Prot entry NADK_PYRHO

assay_conditions_summary: pH 6.8; 343.15 K; cofactor NAD+


organism: Salmonella typhimurium

sequence_source: UniProtKB direct REST lookup, accession P65774, reviewed Swiss-Prot entry NADK_SALTY


organism: Sphingomonas sp.

sequence_source: UniProtKB direct REST lookup, accession Q6L7J5, unreviewed TrEMBL entry Q6L7J5_9SPHN

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Staphylococcus aureus

sequence_source: UniProtKB direct REST lookup, accession H6UH60, unreviewed TrEMBL entry H6UH60_STAAU

proof_lines: recombinant enzyme, pH and temperature not specified in the publication


substrate_name: NADP+

proof_lines: wild-type enzyme, pH and temperature not specified in the publication

substrate: NADP+


organism: Entamoeba histolytica

sequence_source: UniProtKB:C4LSN1 REST direct check on 2026-06-03

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


substrate_name: NADH

substrate: NADH


organism: Escherichia coli

sequence_source: UniProtKB:P0A7B3 REST direct check on 2026-06-03

assay_conditions_summary: cofactor NADP+


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7B3 REST direct check on 2026-06-03 and applied mutation signature R175G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: NAD+ kinase(Enzyme) mutant R175G


organism: Homo sapiens

sequence_source: UniProtKB:O95544 REST direct check on 2026-06-03

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


sequence_source: UniProtKB:Q4G0N4 REST direct check on 2026-06-03


organism: Listeria monocytogenes

sequence_source: UniProtKB:Q8Y8D7 REST direct check on 2026-06-03

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: in 50 mM Tris-HCl, pH 7.4, 10 mM MgCl2, at 30°C


organism: Listeria monocytogenes serotype 1/2a


organism: Arabidopsis thaliana

sequence_source: UniProtKB REST Q9C5W3; reviewed Swiss-Prot entry NADK2_ARATH, Arabidopsis thaliana, NAD kinase 2, EC 2.7.1.23


sequence_source: UniProtKB REST Q500Y9; reviewed Swiss-Prot entry NADHK_ARATH, Arabidopsis thaliana, NADH kinase, EC 2.7.1.86


sequence_source: UniProtKB REST Q56YN3; reviewed Swiss-Prot entry NADK1_ARATH, Arabidopsis thaliana, NAD(H) kinase 1, EC 2.7.1.23 and EC 2.7.1.86


organism: Bacillus subtilis

sequence_source: UniProtKB REST O31612; reviewed Swiss-Prot entry NADK1_BACSU, Bacillus subtilis strain 168, NAD kinase 1, EC 2.7.1.23

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+


sequence_source: UniProtKB REST C4LSN1; active TrEMBL entry C4LSN1_ENTH1, Entamoeba histolytica strain HM-1:IMSS, inorganic polyphosphate/ATP-NAD kinase putative


proof_lines: with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C

proof_lines: with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C


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


substrate_name: NAD(+)

substrate: NAD(+)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: NAD (with 5 mM ATP as phosphoryl donor at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7; cofactor ATP


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: ATP (at pH 6 and 70 degrees Celsius)

assay_conditions_summary: pH 6; cofactor ATP

substrate: ATP (at pH 6 and 70 degrees Celsius)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NAD

assay_conditions_summary: cofactor ATP

substrate: NAD


assay_conditions_summary: pH 7.9; cofactor ATP

proof_lines: Measured at pH 7.9 and 25 degrees Celsius for all experiments.


organism: Bacillus subtilis (strain 168)

substrate_name: NAD (at pH 7.8 and 25 degrees Celsius)

proof_lines: kcat is 8 sec(-1) for kinase activity with NAD (at pH 7.8 and 25 degrees Celsius).

substrate: NAD (at pH 7.8 and 25 degrees Celsius)


organism: Escherichia coli (strain K12)

substrate_name: NAD (at pH 7 and 37 degrees Celsius)

proof_lines: kcat is 55 sec(-1) for kinase activity with ATP. kcat is 125 sec(-1) for kinase activity with NAD.

substrate: NAD (at pH 7 and 37 degrees Celsius)


organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

substrate_name: ATP (at pH 7.5 and 30 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 13.78 sec(-1) for kinase activity with ATP (at pH 7.5 and 30 degrees Celsius). kcat is 13.12 sec(-1) for kinase activity with NAD (at pH 7.5 and 30 degrees Celsius).

substrate: ATP (at pH 7.5 and 30 degrees Celsius)


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius)

assay_conditions_summary: pH 8.5; cofactor ATP

proof_lines: kcat is 399 sec(-1) for kinase activity with ATP as substrate. kcat is 424 sec(-1) for kinase activity with NAD as substrate. kcat is 906 sec(-1) for phosphatase activity with fructose 1,6-bisphosphate and NADP as substrates. kcat is 1007 s


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


assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

proof_lines: calmodulin-dependent isoform, pH 7.9, 25°C


organism: Azotobacter vinelandii

assay_conditions_summary: 310.15 K; cofactor NAD+


organism: Bacillus licheniformis

assay_conditions_summary: pH 6.8; cofactor NAD+


assay_conditions_summary: cofactor NAD+


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP

proof_lines: in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C

proof_lines: in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


organism: Corynebacterium glutamicum subsp. lactofermentum

assay_conditions_summary: pH 6; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme P57S/P117S, at pH 6.0 and 30°C

proof_lines: mutant enzyme P57S/P117S, at pH 7.5 and 30°C


organism: Escherichia coli

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+


organism: Gallus gallus

proof_lines: enzyme immobilized on CNBr-activated Sepharose 4B


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines:
in 100 mM Tris-HCl (pH 8.0), at 37°C
at pH 8.0 and 50°C
pH 7.4, 30°C


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines:
pH 8
ATP in form of MgATP2-


organism: Listeria monocytogenes


proof_lines: wild-type, in the presence of 0.5 mM ATP


proof_lines: mutant D45N, in the presence of 0.5 mM ATP

proof_lines: mutant D45N, in the presence of 4 mM ATP


organism: Mycobacterium tuberculosis

proof_lines: cosubstrate polyphosphate, mutant T195A, 37°C, pH 8.0

proof_lines: cosubstrate ATP, mutant T195A, 37°C, pH 8.0


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Solanum pimpinellifolium

proof_lines:
pH 7.5, 30°C
ATP in form of MgATP2-


organism: Strongylocentrotus purpuratus


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB Q58327 direct EC+organism lookup; PMID 16192277 supports MJ0917 NAD kinase activity.

assay_conditions_summary: pH 8.5; 358.15 K; cofactor NAD+


organism: Micrococcus flavus

proof_lines: pH 7.0, 37°C, cosubstrate ATP, mutant G183R

proof_lines: pH 7.0, 37°C, cosubstrate poly(P)4, mutant G183R


proof_lines: pH 7.0, 37°C, cosubstrate poly(P)4, wild-type

proof_lines: pH 7.0, 37°C, cosubstrate ATP, wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHV7 direct EC+organism lookup; PMID 15182203 mutagenesis feature supports S199A. and applied mutation signature S199A to reconstruct the assayed variant sequence.

proof_lines: cosubstrate ATP, mutant S199A, 37°C, pH 8.0

proof_lines: cosubstrate polyphosphate, mutant S199A, 37°C, pH 8.0


sequence_source: UniProtKB P9WHV7 direct EC+organism lookup; PMID 15182203 supports Mycobacterium tuberculosis NAD kinase activity.

proof_lines: cosubstrate polyphosphate, wild-type, 37°C, pH 8.0

proof_lines: cosubstrate ATP, wild-type, 37°C, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHV7 direct EC+organism lookup; PMID 15182203 mutagenesis feature supports G208A. and applied mutation signature G208A to reconstruct the assayed variant sequence.

proof_lines: cosubstrate polyphosphate, mutant G208A, 37°C, pH 8.0

proof_lines: cosubstrate ATP, mutant G208A, 37°C, pH 8.0


organism: Populus trichocarpa

substrate_name: L-quinate

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

assay_conditions_summary: pH 8.5; 295.15 K; cofactor NAD+

proof_lines:
with NAD+, isozyme Poptr3, pH 8.5, 22°C
with NAD+, isozyme Poptr2, pH 8.5, 22°C

substrate: L-quinate


organism: Escherichia coli (strain K12)

assay_conditions_summary: pH 9

proof_lines: kcat is 91 sec(-1) for dehydrogenase activity with shikimate (at pH 9 and 20 degrees Celsius). kcat is 113 sec(-1) for dehydrogenase activity with quinate (at pH 9 and 20 degrees Celsius). kcat is 105 sec(-1) for dehydrogenase activity with


substrate_name: shikimate

sequence_variant_note: Resolved canonical sequence from UniProt P0A6D5 FASTA direct lookup; mutant rows reconstructed from the checked canonical sequence. and applied mutation signature S67A to reconstruct the assayed variant sequence.

substrate: shikimate


sequence_source: UniProt P0A6D5 FASTA direct lookup; mutant rows reconstructed from the checked canonical sequence.

assay_conditions_summary: pH 9; 293.15 K; cofactor NAD+

proof_lines: wild type enzyme, in the presence of shikimate, 20°C, pH 9.0

proof_lines: wild type enzyme, in the presence of L-quinate, 20°C, pH 9.0


substrate_name: NAD+; Shikimate

sequence_variant_note: Resolved canonical sequence from UniProt P0A6D5 FASTA direct lookup; mutant rows reconstructed from the checked canonical sequence. and applied mutation signature D107A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant D107A

proof_lines: mutant D107A, in the presence of shikimate, 20°C, pH 9.0

substrate: NAD+; Shikimate


sequence_variant_note: Resolved canonical sequence from UniProt P0A6D5 FASTA direct lookup; mutant rows reconstructed from the checked canonical sequence. and applied mutation signature Q262A to reconstruct the assayed variant sequence.


substrate_name: NAD+


sequence_variant_note: Resolved canonical sequence from UniProt P0A6D5 FASTA direct lookup; mutant rows reconstructed from the checked canonical sequence. and applied mutation signature Y39F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P0A6D5 FASTA direct lookup; mutant rows reconstructed from the checked canonical sequence. and applied mutation signature S22A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_lookup_plus_reconstructed_variant and applied mutation signature T106A to reconstruct the assayed variant sequence.


substrate_name: Quinate

sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_lookup_plus_reconstructed_variant and applied mutation signature S22A to reconstruct the assayed variant sequence.

substrate: Quinate


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_lookup_plus_reconstructed_variant and applied mutation signature S67A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_lookup_plus_reconstructed_variant and applied mutation signature Q262A to reconstruct the assayed variant sequence.


substrate_name: NAD+; Quinate

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant S67A

proof_lines: mutant S67A, in the presence of L-quinate, 20°C, pH 9.0

substrate: NAD+; Quinate


substrate_name: Quinate; NAD+

sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_lookup_plus_reconstructed_variant and applied mutation signature K71A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant K71A

proof_lines: mutant K71A, in the presence of L-quinate, 20°C, pH 9.0

proof_lines: mutant K71A, in the presence of shikimate, 20°C, pH 9.0

substrate: Quinate; NAD+


substrate: NAD+


organism: Pseudomonas putida

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

assay_conditions_summary: pH 8.8; 298.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0A6D5 and applied mutation signature Q262A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant Q262A

proof_lines: mutant Q262A, in the presence of L-quinate, 20°C, pH 9.0


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0A6D5 and applied mutation signature T106A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant T106A

proof_lines: mutant T106A, in the presence of L-quinate, 20°C, pH 9.0


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0A6D5 and applied mutation signature Y39F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant Y39F

proof_lines: mutant Y39F, in the presence of shikimate, 20°C, pH 9.0


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0A6D5 and applied mutation signature S22A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: quinate/shikimate dehydrogenase(Enzyme) mutant S22A

proof_lines: mutant S22A, in the presence of shikimate, 20°C, pH 9.0


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0A6D5 and applied mutation signature S67A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0A6D5 and applied mutation signature K71A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q9X5C9 direct REST check on 2026-06-03


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


sequence_source: UniProtKB reviewed A4QB65 direct REST check on 2026-06-03

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

proof_lines: pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+


assay_conditions_summary: pH 8.6; 303.15 K; cofactor NAD+

proof_lines:
with NAD+, pH 8.6, 30°C
pH 9.0-9.5, 30°C, with NAD+
pH 9.0-9.5, 30°C, with quinate


sequence_source: UniProtKB reviewed P0A6D5 direct REST check on 2026-06-03


substrate_name: NADP+; Shikimate

assay_conditions_summary: pH 9; 293.15 K; cofactor NADP+

proof_lines: pH 9, 20°C, cosubstrate shikimate or L-quinate

substrate: NADP+; Shikimate


substrate_name: NADP+


organism: Rhodococcus rhodochrous

substrate_name: beta-NAD+

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

assay_conditions_summary: pH 10; cofactor NAD+

proof_lines:
pH 10, cosubstrate (-)-quinate
pH 10, (-)-enantiomer, cosubstrate NAD+

substrate: beta-NAD+


organism: Brassica napus

assay_conditions_summary: cofactor NADP+

proof_lines: with quinate, pH and temperature not specified in the publication

proof_lines: with shikimate, pH and temperature not specified in the publication

proof_lines: with NAD+, pH and temperature not specified in the publication

substrate: NADP+


organism: Brassica rapa


organism: Escherichia coli

sequence_source: UniProtKB reviewed accession P0A6D5 (YDIB_ECOLI), EC 1.1.1.282 evidence includes PMID 12637497; canonical sequence retrieved 2026-06-03

proof_lines:
pH 9, 20°C, cosubstrate shikimate
pH 9, 20°C, cosubstrate NAD+
pH 9, 20°C, cosubstrate NADP+


organism: Neurospora crassa


organism: Nicotiana tabacum

assay_conditions_summary: cofactor NAD+


organism: Pinus taeda

assay_conditions_summary: pH 10; 293.15 K; cofactor NADP+

proof_lines: pH 10, 20°C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase

proof_lines: pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase

proof_lines: pH 10, 20°C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase


sequence_source: UniProtKB direct lookup: Q88JP1


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADP+


proof_lines:
pH 8.8, 25°C, with shikimate
pH 8.8, 25°C, with NAD+
pH 8.8, 25°C, with NADP+


organism: Pseudomonas putida KT2440

substrate_name: quinate

sequence_source: UniProtKB direct lookup: Q88K85

proof_lines:
in the presence of 2 mM NAD+
in the presence of quinate
in the presence of shikimate

substrate: quinate


organism: Solanum lycopersicum

sequence_source: UniProtKB direct lookup: A0A3Q7H2B2

proof_lines: with NADP+, pH and temperature not specified in the publication


sequence_source: UniProtKB direct lookup: A0A3Q7IET9


enzyme_display_name: glutaminase

organism: Anabaena sp.

substrate_name: glutamine

proof_lines: Km apparent, no Michaelis-Menten kinetics

enzyme: glutaminase

substrate: glutamine


sequence_source: UniProtKB Q8YSZ5 canonical sequence (release 2026_01)


organism: Arabidopsis thaliana

substrate_name: L-Glutamine; H2O

substrate: L-Glutamine; H2O


substrate_name: L-Glutamine

substrate: L-Glutamine


organism: Aspergillus oryzae

sequence_source: UniProtKB Q2U4L7 canonical sequence (release 2026_01)


organism: Bacillus subtilis


sequence_source: UniProtKB O07637 canonical sequence (release 2026_01)


sequence_source: UniProtKB O31465 canonical sequence (release 2026_01)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 FASTA; N248Q reconstructed using UniProt chain start 23 so mature residue N248 maps to canonical residue N270. and applied mutation signature N248Q with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant N248Q


substrate_name: H2O; L-Glutamine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 FASTA; N248A reconstructed using UniProt chain start 23 so mature residue N248 maps to canonical residue N270. and applied mutation signature N248A with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant N248A

substrate: H2O; L-Glutamine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 FASTA; N248D reconstructed using UniProt chain start 23 so mature residue N248 maps to canonical residue N270. and applied mutation signature N248D with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00805 FASTA canonical sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77454 exact accession lookup; row sequence reconstructed from canonical P77454 with Q162A. and applied mutation signature Q162A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant YbaS Q162A His6-tagged


substrate_name: L-glutamine

sequence_source: UniProtKB:P77454 exact accession lookup; canonical sequence retained as identity context only.

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

substrate: L-glutamine


sequence_source: UniProtKB:P77454 exact accession lookup.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77454 exact accession lookup; row sequence reconstructed from canonical P77454 with G261A. and applied mutation signature G261A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant YbaS G261A His6-tagged


sequence_source: UniProtKB:P0A6W0 exact accession lookup.


organism: Geobacillus thermodenitrificans

sequence_source: UniProtKB:A4IPX2 exact accession lookup.


organism: Helicobacter pylori

substrate_name: L-Asparagine

substrate: L-Asparagine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature N248D with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant N248D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature V27M with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature V27L with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature Q59G with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature Q59E with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant Q59E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature N248E with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348 and applied mutation signature G57V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant G57V


sequence_source: UniProtKB:P00805 direct lookup; variant reconstructed with mature-chain numbering offset +22 from UniProt signal peptide 1-22 and chain 23-348

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant V27L


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature Q59A with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant Q59A


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature G57A with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature V27M with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant V27M


sequence_source: UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22.


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature N248E with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant N248E


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature Q59G with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant Q59G


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature N248Q with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P00805 REST FASTA; variant reconstructed from selected mutation signature with mature-chain offset +22 from UniProt signal peptide 1-22. and applied mutation signature Q59E with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


organism: Homo sapiens

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

proof_lines: pH 8.5, temperature not specified in the publication, isozyme GLS2

proof_lines: lower than, soluble and membrane-associated N-PAG, 37°C, pH 8.6

proof_lines: brain, membrane-associated PAG, 37°C, pH 8.6


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

proof_lines: wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C


proof_lines: mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C


substrate_name: L-asparagine

proof_lines: mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C

substrate: L-asparagine


proof_lines: mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C


proof_lines: mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProt O94925-3 FASTA; reconstructed F318Y/F322S after direct residue check; PubMed 22049910 and RCSB 3UNW/3UO9 anchor to O94925/GAC. and applied mutation signature F322S/F318Y to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) wildtype GLS1 splice variant GAC, His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt O94925-3 FASTA; reconstructed Y394L after direct residue check; PubMed 22049910 and RCSB 3UNW/3UO9 anchor to O94925/GAC. and applied mutation signature Y394L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant Y394L, GLS1 splice variant GAC, His-tagged

proof_lines: pH 8.5, temperature not specified in the publication, GAC mutant Y394L


sequence_source: UniProt O94925-3 FASTA direct accession/isoform lookup for wild-type GAC.

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

proof_lines: pH 8.5, temperature not specified in the publication, wild-type GAC and GAC mutant F322S/F318Y


sequence_source: UniProt O94925-3 FASTA; PubMed 22049910 and RCSB 3UNW/3UO9 anchor to O94925/GAC.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94925 canonical sequence from REST lookup on 2026-06-03, reconstructed with source mutation Y394L and applied mutation signature Y394L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94925 canonical sequence from REST lookup on 2026-06-03, reconstructed with source mutation F322S/F318Y and applied mutation signature F322S/F318Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant F322S/F318Y, GLS1 splice variant GAC, His-tagged

proof_lines: pH 8.5, temperature not specified in the publication, GAC mutant F322S/F318Y


sequence_source: UniProtKB:Q9UI32 canonical sequence from REST lookup on 2026-06-03


sequence_source: UniProtKB:O94925 canonical sequence from REST lookup on 2026-06-03

proof_lines: pH 8.5, temperature not specified in the publication, isozyme GLS1


organism: Lactococcus lactis

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant R433M


proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant T431V


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I387 canonical sequence from REST lookup on 2026-06-03


organism: Rattus norvegicus

sequence_source: UniProtKB:P28492 direct REST lookup on 2026-06-03


organism: Saccharomyces cerevisiae


organism: Synechocystis sp. PCC 6803

sequence_source: UniProtKB:P73903 direct REST lookup on 2026-06-03

proof_lines:
1 mol/l NaCl present
Km apparent, no Michaelis-Menten enzyme


organism: Bizionia argentinensis

sequence_source: UniProtKB G2EHQ3 direct REST lookup; release header 2026_01; live TrEMBL glutaminase entry with EC 3.5.1.2.


organism: Cohnella sp. A01

sequence_source: NCBI Protein QCI03326.1 efetch plus UniParc UPI0010C3FF63 archived sequence for deleted UniProtKB A0A4D6WPI1; no active UniProtKB replacement found.


organism: Escherichia coli

sequence_source: UniProtKB P00805 direct REST lookup; reviewed Swiss-Prot L-asparaginase 2 entry with EC 3.5.1.1 and signal peptide/chain features checked.

column_label: Table 2 (Protein Science 2000, 9:2009-2017): kinetic constants for the hydrolysis of L-asparagine and L-glutamine at pH 7.0 and 25 degrees C, L-Glutamine block; row Table 2 decoded row, wild-type EcA2, L-Glutamine columns; column 'kcat (s^-1)' = 3.3 x 10^-1; column 'Km (mol L^-1)' = 3.5 x 10^-3; column 'kcat/Km (M^-1 s^-1)' = 9.4 x 10^1.

normalized_value_unit_evidence: kcat: printed cell 3.3 x 10^-1 s^-1 is already in s^-1, so no unit conversion applies and the canonical value is 0.33 s^(-1). Km: printed cell 3.5 x 10^-3 mol L^-1; one mol L^-1 is 1000 mM, so 0.0035 x 1000 = 3.5 mM. kcat/Km: printed cell 9.4 x 10^1 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 94.0 / 1000 = 0.094 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (Protein Science 2000, 9:2009-2017): kinetic constants for the hydrolysis of L-asparagine and L-glutamine at pH 7.0 and 25 degrees C, L-Glutamine block; Table 2 decoded row, wild-type EcA2, L-Glutamine columns; column kcat (s^-1) prints 3.3 x 10^-1; column Km (mol L^-1) prints 3.5 x 10^-3; column kcat/Km (M^-1 s^-1) prints 9.4 x 10^1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00805 canonical precursor plus selected mutation N248G; UniProt signal peptide 1-22 means mature residue 248 maps to precursor position 270. and applied mutation signature N248G with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant N248G


sequence_variant_note: Resolved canonical sequence from UniProtKB P00805 canonical precursor plus selected mutation G57V; UniProt signal peptide 1-22 means mature residue 57 maps to precursor position 79. and applied mutation signature G57V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00805 canonical precursor plus selected mutation N248A; UniProt signal peptide 1-22 means mature residue 248 maps to precursor position 270. and applied mutation signature N248A with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P00805 canonical precursor plus selected mutation N248G; UniProt signal peptide 1-22 means mature residue 248 maps to precursor position 270.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00805 canonical precursor plus selected mutation G57A; UniProt signal peptide 1-22 means mature residue 57 maps to precursor position 79. and applied mutation signature G57A with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant G57A


organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)


organism: Bacillus subtilis (strain 168)


organism: Escherichia coli (strain K12)


sequence_source: source_record identity cache for UniProtKB:O94925


substrate_name: dihydroorotate

sequence_source: source_record identity cache for UniProtKB:P27708

substrate: dihydroorotate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

sequence_source: source_record identity cache for UniProtKB:Q03144


sequence_source: source_record identity cache for UniProtKB:P07259