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.


enzyme_display_name: deoxynucleoside kinase

organism: Drosophila melanogaster

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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.

mutation_type: substitution

enzyme: deoxynucleoside kinase

source: brenda


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.


source_db: oed

verification_status: unverified

mutation_signature: Unknown

kcat_over_km_origin: calculated

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.

data_origin: experimental

status: unverified

source: oed


substrate_name: Cytarabine

substrate: Cytarabine


substrate_name: deoxyadenosine

substrate: deoxyadenosine


substrate_name: thymidine

substrate: thymidine


organism: Xenopus laevis

substrate_name: Thymidine; ATP

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

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

assay_conditions_summary: cofactor ATP

substrate: Thymidine; ATP


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

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

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

source_databases_merged: brenda skid


organism: Natranaerobius thermophilus

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


organism: Neurospora crassa

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

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

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

sequence_source: UniProtKB: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

source_databases_merged: sabio_rk brenda skid


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


km_display: Not reported

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

source_db: uniprot

substrate: shikimate

source: uniprot


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)

assay_conditions_summary: pH 8


verification_status: corrected

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.

status: corrected


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

ki_unit: mM

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


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

verification_status: verified

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.

status: verified


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


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

sequence_source: source_record identity cache for UniProtKB:Q8DNZ8


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

sequence_source: source_record identity cache for UniProtKB:Q9X0C8


organism: Acinetobacter glutaminasificans

substrate_name: L-Gln

substrate: L-Gln


organism: Aspergillus flavus


organism: Aspergillus fumigatus

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


organism: Aspergillus oryzae


organism: Aspergillus sojae


organism: Bacillus cereus


organism: Arabidopsis thaliana


substrate_name: ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 2.49 sec(-1) for FGAM synthase activity (at pH 7.2 and 37 degrees Celsius). kcat is 0.002 sec(-1) for glutaminase activity (at pH 7.2 and 37 degrees Celsius).


proof_lines: kcat is 7.60 min(-1) for glutaminase activity.


organism: Plasmodium falciparum (isolate 3D7)


organism: Sporosarcina pasteurii

substrate_name: L-Asn

proof_lines:
pH 9.0, at 37ºC, H2O as co-substrate
pH 9.0, at 37ºC, NH2OH as co-substrate

substrate: L-Asn


organism: Streptomyces roseolus

substrate_name: L-Glutamic acid

substrate: L-Glutamic acid


organism: Streptomyces sp.

substrate_name: L-glutamate

substrate: L-glutamate


organism: Trichoderma reesei

proof_lines: polyacrylic acid-Cu2+-immobilized enzyme, at pH 8.0 and 50°C


organism: Bacillus sp. (in: firmicutes)


organism: Camelus dromedarius


organism: Escherichia coli

substrate_name: gamma-glutamyl methylamide

substrate: gamma-glutamyl methylamide


organism: Geobacillus sp. H6a


organism: Lacticaseibacillus rhamnosus

assay_conditions_summary: pH 7


organism: Limosilactobacillus reuteri


organism: Pseudomonas aeruginosa


organism: Pseudomonas chlororaphis subsp. aurantiaca


organism: Rattus norvegicus

mutation_type: deletion

assay_conditions_summary: pH 8; buffer acetate/phosphate

proof_lines: recombinant enzyme with N-terminal deletion, T-acetate buffer, pH 8.0

proof_lines: recombinant enzyme with N-terminal deletion, T-phosphate buffer, pH 8.0


assay_conditions_summary: pH 8; buffer phosphate/acetate

proof_lines: recombinant enzyme with N-terminal and C-terminal deletions, T-phosphate buffer, pH 8.0

proof_lines: recombinant enzyme with N-terminal and C-terminal deletions, T-acetate buffer, pH 8.0


substrate_name: Gln

assay_conditions_summary: pH 8

proof_lines:
in presence of 150 mM phosphate
native enzyme, T-acetate buffer, pH 8.0
in presence of 10 mM phosphate

substrate: Gln


organism: Rhizobium etli

substrate_name: Unknown

substrate: Unknown


organism: Micrococcus luteus

proof_lines: pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl

proof_lines: pH 7.5, 30°C, full-length enzyme, in absence of NaCl

proof_lines: pH 7.5, 30°C, protease-cleaved large enzyme fragment, in absence of NaCl


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence, reconstructed with selected source mutation Y191T. and applied mutation signature Y191T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence, reconstructed with selected source mutation E160D. and applied mutation signature E160D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence, reconstructed with selected source mutation Y191F. and applied mutation signature Y191F to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: succinamate

proof_lines: pH and temperature not specified in the publication

substrate: succinamate


sequence_source: UniProtKB P17169 canonical sequence checked 2026-06-03; A602L variant requires manual processed-chain coordinate arbitration.

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

assay_conditions_summary: Glutaminase activity measured as Gln hydrolysis in absence of Fru-6P.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant A602L


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature W74L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant W74L


sequence_source: UniProtKB P17169 REST/FASTA checked 2026-06-03.


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature W74F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant W74F


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature W74A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant W74A


sequence_source: UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants.


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature V605L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant V605L


enzyme_display_name: aspartate carbamoyltransferase

organism: Homo sapiens

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

enzyme: aspartate carbamoyltransferase


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

assay_conditions_summary: cofactor ATP


organism: Bacillus subtilis

substrate_name: Carbamoyl phosphate; L-Aspartate

sequence_source: UniProtKB:P05654 FASTA retrieved 2026-06-03

substrate: Carbamoyl phosphate; L-Aspartate


organism: Enterococcus faecalis

substrate_name: L-Aspartate; Carbamoyl phosphate

sequence_source: UniProtKB:Q9L4T8 FASTA retrieved 2026-06-03

substrate: L-Aspartate; Carbamoyl phosphate


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

sequence_source: UniProtKB:P0A786 FASTA retrieved 2026-06-03

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=8.3


organism: Mesocricetus auratus

proof_lines: SABIO-RK modifier species: aspartate carbamoyltransferase(Enzyme) mutant D90A N-terminal His6-tag


proof_lines: SABIO-RK modifier species: aspartate carbamoyltransferase(Enzyme) mutant R269A N-terminal His6-tag


substrate_name: L-Aspartate

sequence_source: UniProtKB:P08955 FASTA retrieved 2026-06-03

substrate: L-Aspartate


substrate_name: Carbamoyl phosphate

smiles: NC(=O)OP(=O)(O)O

substrate: Carbamoyl phosphate


enzyme_display_name: histidine decarboxylase

organism: Clostridium perfringens

substrate_name: L-Histidine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature K172I with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant K172I

enzyme: histidine decarboxylase

substrate: L-Histidine


sequence_source: UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22

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 REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature S96T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S96T


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature Y280F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant Y280F


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature I74E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant I74E


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature F98A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant F98A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature E81Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E81Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature Y77F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant Y77F


organism: Lactobacillus sp.

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature E197D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E197D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature E66Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E66Q


sequence_source: UniProtKB:P00862 REST direct check on 2026-06-03


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature E197Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E197Q


sequence_variant_note: Mutation signature S82C matches the mutant residue at offset +1 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S82C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature S82T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S82T


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P00862 sequence with reviewer-computed S82T substitution and applied mutation signature S82T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P00862 sequence with reviewer-computed S82C substitution and applied mutation signature S82C to reconstruct the assayed variant sequence.


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

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant G58D


sequence_source: UniProt REST accession P00862 reviewed canonical sequence fetched during worker7 review

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=4.8


organism: Morganella morganii

sequence_source: UniProt REST accession P05034 reviewed canonical sequence fetched during worker7 review


sequence_source: UniProt REST accession P23738 reviewed canonical sequence fetched during worker7 review


organism: Oenococcus oeni

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


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

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E214H


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S97T


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E214D


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant D78A


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E214I


substrate_name: L-Histidine; L-Dopa

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant C-terminal truncated (2-477)

substrate: L-Histidine; L-Dopa


sequence_variant_note: Mutation signature S354G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant C180S/C418S C-terminal truncated (2-477)


substrate_name: L-histidine

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

substrate: L-histidine


substrate_name: L-Dopa

substrate: L-Dopa


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S354G C-terminal truncated (2-477)


mutation_signature: truncation

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.8
Raw SKiD Env: Temp=-----, pH=-----


organism: Lactobacillus buchneri


organism: Lactobacillus sp. (strain 30a)


substrate_name: histidine

substrate: histidine


sequence_source: UniProtKB:P16453 canonical displayed sequence


enzyme_display_name: carboxymethylproline synthase

organism: Pectobacterium carotovorum subsp. carotovorum

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 sec(-1) with malonyl-CoA as substrate. kcat is 1.52 sec(-1) with (S)-1-pyrroline-5-carboxylate as substrate.

enzyme: carboxymethylproline synthase

substrate: malonyl-CoA


organism: Pectobacterium carotovorum

sequence_source: UniProtKB reviewed accession Q9XB60 from direct EC/name/organism lookup on 2026-06-03

assay_conditions_summary: pH 7.8; 295.15 K; buffer a piperazine/HEPES; cofactor CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'malonyl-CoA' whose reaction cell reads (2S,5S)-CMPr formation; column 'kcat (s-1)' = 1.7 ± 0.2; column 'Km (mM)' = 0.0027 ± 0.0009; column 'kcat/Km (mM-1 s-1)' = 630.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.0027 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.0027 mM; the exported value is 0.0015 mM, which Table 1 prints in its L-P5C body row. kcat: printed Table 1 cell 1.7 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.7 s^(-1); the exported value is 1.7 s^(-1). kcat/Km: printed Table 1 cell 630 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 630.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 1.7 / 0.0027 = 629.6296296296297 s^-1 mM^-1, and the article's own printed efficiency cell is 630 s^-1 mM^-1, which this record carries.

raw_value_unit_evidence: Table 1, body row 'malonyl-CoA', reaction '(2S,5S)-CMPr formation': kcat = 1.7 ± 0.2 s^-1; Km = 0.0027 ± 0.0009 mM; printed kcat/Km = 630 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'malonyl-CoA' and reaction '(2S,5S)-CMPr formation'

table_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0 (Biochemistry 2004, volume 43, issue 50, pages 15936-15945)


enzyme_display_name: Carboxymethylproline synthase

organism: Erwinia carotovora

substrate_name: Malonyl-CoA

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA

enzyme: Carboxymethylproline synthase

substrate: Malonyl-CoA


assay_conditions_summary: pH 8; 295.15 K; buffer a piperazine/HEPES; cofactor CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'L-pyrroline-5-carboxylate'; column 'reaction' = (2S,5S)-CMPr formation; column 'kcat (s-1)' = 1.52 ± 0.04; column 'Km (mM)' = 0.0015 ± 0.0004; column 'kcat/Km (mM-1 s-1)' = 984.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.0015 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.0015 mM; the exported value is 0.002 mM. kcat: printed Table 1 cell 1.52 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.52 s^(-1); the exported value is 1.52 s^(-1). kcat/Km: printed Table 1 cell 984 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 984.0 s^(-1)*mM^(-1); the exported value is 760.0 s^(-1)*mM^(-1), the quotient of the exported kcat and the exported Km. Closure disclosure: the quotient of the two printed component cells is 1.52 / 0.0015 = 1013.3333333333334 s^-1 mM^-1, and the article's own printed efficiency cell is 984 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'L-pyrroline-5-carboxylate', reaction '(2S,5S)-CMPr formation': kcat = 1.52 ± 0.04 s^-1; Km = 0.0015 ± 0.0004 mM; printed kcat/Km = 984 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'L-pyrroline-5-carboxylate' and reaction '(2S,5S)-CMPr formation'


substrate_name: Propanoyl-CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'propionyl-CoA'; column 'reaction' = hydrolysis; column 'kcat (s-1)' = 0.190 ± 0.009; column 'Km (mM)' = 1.7 ± 0.2; column 'kcat/Km (mM-1 s-1)' = 0.110.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.7 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.7 mM; the exported value is 1.7 mM. kcat: printed Table 1 cell 0.190 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.19 s^(-1); the exported value is 0.19 s^(-1). kcat/Km: printed Table 1 cell 0.110 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.11 s^(-1)*mM^(-1); the exported value is 0.11176470588235295 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.19 / 1.7 = 0.11176470588235295 s^-1 mM^-1, and the article's own printed efficiency cell is 0.110 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'propionyl-CoA', reaction 'hydrolysis': kcat = 0.190 ± 0.009 s^-1; Km = 1.7 ± 0.2 mM; printed kcat/Km = 0.110 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'propionyl-CoA' and reaction 'hydrolysis'

substrate: Propanoyl-CoA


substrate_name: Acetyl-CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'acetyl-CoA'; column 'reaction' = hydrolysis; column 'kcat (s-1)' = 0.043 ± 0.002; column 'Km (mM)' = 5.4 ± 0.7; column 'kcat/Km (mM-1 s-1)' = 0.0081.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.4 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 5.4 mM; the exported value is 5.4 mM. kcat: printed Table 1 cell 0.043 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.043 s^(-1); the exported value is 0.043 s^(-1). kcat/Km: printed Table 1 cell 0.0081 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.0081 s^(-1)*mM^(-1); the exported value is 0.007962962962962962 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.043 / 5.4 = 0.007962962962962962 s^-1 mM^-1, and the article's own printed efficiency cell is 0.0081 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'acetyl-CoA', reaction 'hydrolysis': kcat = 0.043 ± 0.002 s^-1; Km = 5.4 ± 0.7 mM; printed kcat/Km = 0.0081 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'acetyl-CoA' and reaction 'hydrolysis'

substrate: Acetyl-CoA


column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'methylmalonyl-CoA' carrying footnote marker c; column 'reaction' = decarboxylation; column 'kcat (s-1)' = 0.07 ± 0.01; column 'Km (mM)' = 0.6 ± 0.3; column 'kcat/Km (mM-1 s-1)' = 0.10.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.6 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.6 mM; the exported value is 0.6 mM. kcat: printed Table 1 cell 0.07 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.07 s^(-1); the exported value is 0.07 s^(-1). kcat/Km: printed Table 1 cell 0.10 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.1 s^(-1)*mM^(-1); the exported value is 0.11666666666666668 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.07 / 0.6 = 0.11666666666666668 s^-1 mM^-1, and the article's own printed efficiency cell is 0.10 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'methylmalonyl-CoA', reaction 'decarboxylation': kcat = 0.07 ± 0.01 s^-1; Km = 0.6 ± 0.3 mM; printed kcat/Km = 0.10 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'methylmalonyl-CoA' and reaction 'decarboxylation'


substrate_name: Carboxymethylproline-CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'CMPr-CoA'; column 'reaction' = hydrolysis; column 'kcat (s-1)' = 0.53 ± 0.05; column 'Km (mM)' = 0.009 ± 0.002; column 'kcat/Km (mM-1 s-1)' = 58.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.009 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.009 mM; the exported value is 0.009 mM. kcat: printed Table 1 cell 0.53 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.53 s^(-1); the exported value is 0.53 s^(-1). kcat/Km: printed Table 1 cell 58 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 58.0 s^(-1)*mM^(-1); the exported value is 58.88888888888889 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.53 / 0.009 = 58.88888888888889 s^-1 mM^-1, and the article's own printed efficiency cell is 58 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'CMPr-CoA', reaction 'hydrolysis': kcat = 0.53 ± 0.05 s^-1; Km = 0.009 ± 0.002 mM; printed kcat/Km = 58 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'CMPr-CoA' and reaction 'hydrolysis'

substrate: Carboxymethylproline-CoA


enzyme_display_name: steroid 21-monooxygenase

sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature P31Q to reconstruct the assayed variant sequence.

proof_lines: mutant P31Q, pH not specified in the publication, temperature not specified in the publication

enzyme: steroid 21-monooxygenase


substrate_name: progesterone

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature G65E to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'G65E', clinical phenotype column 'SW', substrate column 'progesterone'; column 'kcat' with unit head 'min^-1' = 3.6; column 'Km' with unit head 'uM' = 5.5; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 0.67; column 'Catalytic efficiency' with unit head '% wild type' = 0.082.

normalized_value_unit_evidence: kcat: printed cell 3.6 min^-1; 3.6 / 60 = 0.060000000000000005 s^-1; this pass carries 0.06 s^(-1) and the exported value is 0.062 s^(-1). Km: printed cell 5.5 uM; 5.5 / 1000 = 0.0055 mM; the exported value is 0.0055 mM. kcat/Km: printed cell 0.67 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.67 * 1000 / 60 = 11.166666666666668 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row G65E with substrate progesterone: printed kcat cell 3.6 in the column headed kcat, printed unit min^-1; printed Km cell 5.5 in the column headed Km, printed unit uM; printed kcat/Km cell 0.67 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row G65E with substrate progesterone

table_label: Table 2: Catalytic activities of 21A2 variants (J. Biol. Chem. 2017, 292(26):10767-10778)

substrate: progesterone


sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature V282L to reconstruct the assayed variant sequence.

proof_lines: mutant V282L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature I172N to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'I172N', clinical phenotype column 'SV', substrate column '17alpha-OH-progesterone'; column 'kcat' with unit head 'min^-1' = 0.18; column 'Km' with unit head 'uM' = 4.9; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 0.037; column 'Catalytic efficiency' with unit head '% wild type' = 0.023.

normalized_value_unit_evidence: kcat: printed cell 0.18 min^-1; 0.18 / 60 = 0.003 s^-1; the exported value is 0.003 s^(-1). Km: printed cell 4.9 uM; 4.9 / 1000 = 0.004900000000000001 mM; this pass carries 0.0049 mM and the exported value is 0.0018 mM. kcat/Km: printed cell 0.037 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.037 * 1000 / 60 = 0.6166666666666667 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row I172N with substrate 17alpha-OH-progesterone: printed kcat cell 0.18 in the column headed kcat, printed unit min^-1; printed Km cell 4.9 in the column headed Km, printed unit uM; printed kcat/Km cell 0.037 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row I172N with substrate 17alpha-OH-progesterone


sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature G292C to reconstruct the assayed variant sequence.

proof_lines: mutant G292C, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature L108R to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'L108R', clinical phenotype column 'SW', substrate column 'progesterone'; column 'kcat' with unit head 'min^-1' = 0.0059; column 'Km' with unit head 'uM' = 2.7; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 0.0022; column 'Catalytic efficiency' with unit head '% wild type' = 0.00027.

normalized_value_unit_evidence: kcat: printed cell 0.0059 min^-1; 0.0059 / 60 = 0.00009833333333333333 s^-1; the exported value is 0.0001 s^(-1), which is that quotient at the precision the export carries. Km: printed cell 2.7 uM; 2.7 / 1000 = 0.0027 mM; this pass carries 0.0027 mM and the exported value is 0.0017 mM. kcat/Km: printed cell 0.0022 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.0022 * 1000 / 60 = 0.036666666666666674 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row L108R with substrate progesterone: printed kcat cell 0.0059 in the column headed kcat, printed unit min^-1; printed Km cell 2.7 in the column headed Km, printed unit uM; printed kcat/Km cell 0.0022 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row L108R with substrate progesterone


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature P31L to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'P31L', clinical phenotype column 'NC', substrate column '17alpha-OH-progesterone'; column 'kcat' with unit head 'min^-1' = 84; column 'Km' with unit head 'uM' = 1.7; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 49; column 'Catalytic efficiency' with unit head '% wild type' = 30.

normalized_value_unit_evidence: kcat: printed cell 84 min^-1; 84 / 60 = 1.4 s^-1; the exported value is 1.4 s^(-1). Km: printed cell 1.7 uM; 1.7 / 1000 = 0.0017 mM; this pass carries 0.0017 mM and the exported value is 0.0012 mM. kcat/Km: printed cell 49 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 49 * 1000 / 60 = 816.6666666666667 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row P31L with substrate 17alpha-OH-progesterone: printed kcat cell 84 in the column headed kcat, printed unit min^-1; printed Km cell 1.7 in the column headed Km, printed unit uM; printed kcat/Km cell 49 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row P31L with substrate 17alpha-OH-progesterone


sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature R357W to reconstruct the assayed variant sequence.

proof_lines: mutant R357W, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: mevalonate kinase

substrate_name: Mevalonate; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature T243A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant T243A

enzyme: mevalonate kinase

substrate: Mevalonate; ATP


substrate_name: ATP; Mevalonate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature S146A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant S146A

substrate: ATP; Mevalonate


substrate_name: (R)-mevalonate

sequence_source: UniProtKB Q03426 canonical FASTA retrieved directly for identity context; row-specific variant sequence not reconstructed

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

substrate: (R)-mevalonate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature I56A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature I196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature Y149A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature T104A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; not accepted as row sequence because the selected source context mixes two variants.


sequence_source: UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03.


substrate_name: ATP; (R)-Mevalonate

sequence_source: UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; preserved as identity context only because the selected row does not expose a wild-type or mutation-specific state.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP; (R)-Mevalonate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation D204A. and applied mutation signature D204A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant D204A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation E296Q. and applied mutation signature E296Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant E296Q


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation E193Q. and applied mutation signature E193Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant E193Q


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation E19D. and applied mutation signature E19D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant E19D


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation D204N. and applied mutation signature D204N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant D204N


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature A334T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant A334T chimeric protein with Glutathione S-transferase


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature N301T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant N301T chimeric protein with Glutathione S-transferase


organism: Methanocaldococcus jannaschii

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


organism: Rattus norvegicus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines:
liver mevalonate kinase
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K13M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant K13M


organism: Staphylococcus aureus


enzyme_display_name: sphingosine kinase

organism: Arabidopsis thaliana

substrate_name: Sphingosine kinase 1; Dioleoyl phosphatidic acid

enzyme: sphingosine kinase


organism: Homo sapiens

substrate_name: ATP; Sphingosine

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines:
isoform SphK1, at pH 7.4 and 23Â°C
as bovine serum albumin complex
pH 7.4, 30°C, recombinant isozyme SPHK2

substrate: ATP; Sphingosine


organism: Bos taurus

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P00191, checked 2026-06-03 and applied mutation signature T241R/L442A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession P00191, checked 2026-06-03

proof_lines: pH 7.4, 37°C, CYP21 wild-type and mutant T241R/L442A


substrate_name: H+; Progesterone; NADPH; O2

sequence_source: UniProtKB REST accession P00191, checked 2026-06-03; canonical sequence retained as context only

proof_lines: SABIO-RK modifier species: steroid 21-monooxygenase(Enzyme) mutant C3B21RA N-terminal His6-tag

substrate: H+; Progesterone; NADPH; O2


proof_lines: 37°C, pH 7.4, presence of 0.002% Cymal 5


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P08686, checked 2026-06-03 and applied mutation signature V470A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P08686, checked 2026-06-03 and applied mutation signature V359A to reconstruct the assayed variant sequence.


substrate_name: sphingosine

sequence_source: UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03.

substrate: sphingosine


substrate_name: D-erythro-sphingosine

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature S79A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant S79A

substrate: D-erythro-sphingosine


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature G113A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant G113A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature E180Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant E180Q


sequence_source: Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note.

sequence_variant_note: Mutation signature Δ364 references residue 364, which is outside the resolved sequence length.

proof_lines: pH and temperature not specified in the publication, deletion mutant DELTA364-384


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature E182Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant E182Q


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature K27A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant K27A


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature K29A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant K29A

substrate: ATP


sequence_source: UniProtKB:P08686 direct REST lookup on 2026-06-03

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08686 direct REST lookup plus R409C reconstruction on 2026-06-03 and applied mutation signature R409C to reconstruct the assayed variant sequence.

proof_lines: mutant R409C, pH not specified in the publication, temperature not specified in the publication


organism: Bacopa monnieri

sequence_source: UniProtKB:M1F2U2 direct REST lookup on 2026-06-03


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


organism: Enterococcus faecalis

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:Q03426 direct REST lookup plus S201A reconstruction on 2026-06-03 and applied mutation signature S201A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant S201A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03426 direct REST lookup plus S145A reconstruction on 2026-06-03 and applied mutation signature S145A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant S145A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K103R to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant K103R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D178N to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant D178N


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G26A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant G26A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D176N to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant D176N


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G82A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant G82A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D81N to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D81N enzyme, pH and temperature not specified in the publication


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

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


assay_conditions_summary: pH 7.4; 355.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature V470A/I471A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature V359G to reconstruct the assayed variant sequence.


sequence_source: Direct UniProt REST/FASTA lookup on 2026-06-03: reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence for Homo sapiens CYP21A2, EC 1.14.14.16.


substrate_name: NADPH; H+; O2; Progesterone

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines:
recombinant enzyme, at pH 7.4 and 37°C
pH 7.4, 35°C
pH 7.4, 37°C

substrate: NADPH; H+; O2; Progesterone


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature T296N to reconstruct the assayed variant sequence.

proof_lines: mutant T296N, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature W303R to reconstruct the assayed variant sequence.

proof_lines: mutant W303R, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature G292S to reconstruct the assayed variant sequence.

proof_lines: mutant G292S, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession Q9NRA0 direct lookup on 2026-06-03

proof_lines: in 50 mM HEPES, pH 7.4, 10 mM KCl, 15 mM MgCl2, 0.1% Triton X-100, 20% glycerol, 2 mM orthovanadate, 2 mM dithiothreitol, 10 mM NaF, and 1 mM deoxypyridoxine

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


organism: Mus musculus

substrate_name: Sphingosine; ATP

sequence_source: UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03

substrate: Sphingosine; ATP


sequence_source: UniProtKB reviewed accession Q9JIA7 direct lookup on 2026-06-03

proof_lines: about, pH 7.4, 30°C, recombinant isozyme SPHK1a


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature D175N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.