substrate_name: Ferricytochrome c; Ubiquinol

proof_lines: solubilized in presence of 0.1% bovine serum albumin

substrate: Ferricytochrome c; Ubiquinol


enzyme_display_name: quinol--cytochrome-c reductase

organism: Bacillus sp. (in: firmicutes)

substrate_name: 2 ferricytochrome c1

source_db: brenda

verification_status: unverified

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

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

enzyme: quinol--cytochrome-c reductase

substrate: 2 ferricytochrome c1

status: unverified

source: brenda


enzyme_display_name: cytochrome-c oxidase

organism: Bos taurus

substrate_name: ferrocytochrome c

km_unit: mM

proof_lines: at 7°C, in presence of 56% ethylene glycol

proof_lines: soluble enzyme, higher values for particulate enzyme

enzyme: cytochrome-c oxidase

substrate: ferrocytochrome c


substrate_name: NADH

assay_conditions_summary: pH 7.6; 305.15 K; cofactor NADH

proof_lines: pH 7.6, 32°C, cosubstrate: ubiquinone-1, ubiquinone-0 or idebenone

proof_lines: apparent value, for superoxide production, at 32°C and pH 7.5

substrate: NADH


substrate_name: NMNH

kcat_display: Not reported

assay_conditions_summary: cofactor NADP+

proof_lines: reduction of thio-NADP+ in energized submitochondrial particles

proof_lines: reduction of thio-NADP+ in non energized submitochondrial particles

substrate: NMNH


enzyme_display_name: acetone carboxylase

organism: Rhodobacter capsulatus

substrate_name: acetone

smiles: CC(=O)C

enzyme: acetone carboxylase

substrate: acetone


smiles: O=O


substrate_name: o-Dianisidine

substrate: o-Dianisidine


organism: Carcharhinus acronotus


enzyme_display_name: P-type Na(+) transporter

organism: Enterococcus hirae

substrate_name: Na+/in

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

enzyme: P-type Na(+) transporter

substrate: Na+/in


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines: wild type enzyme, in the presence of Na+, pH and temperature not specified in the publication

proof_lines: wild type enzyme, in the presence of Li+, pH and temperature not specified in the publication

substrate: ATP


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

mutation_type: substitution

proof_lines: mutant enzyme E139D, in the presence of Li+, pH and temperature not specified in the publication

proof_lines: mutant enzyme E139D, in the presence of Na+, pH and temperature not specified in the publication


substrate_name: ubiquinol

substrate: ubiquinol


organism: Thermotoga maritima

substrate_name: Na+[side 1]

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: Na+[side 1]


organism: Bacillus sp. PS3

proof_lines: cytochrome c552 from Thermus thermophilus

proof_lines: cytochrome c551 from thermophilic bacterium PS3


enzyme_display_name: ABC-type Mn(2+) transporter

organism: Synechocystis sp.

enzyme: ABC-type Mn(2+) transporter


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: Na(+)-transporting two-sector ATPase

organism: Dunaliella maritima

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: in the presence of NaCl at 22°C and pH between 7.5 and 8.0

proof_lines: in the presence of Na2SO4 at 22°C and pH between 7.5 and 8.0

enzyme: Na(+)-transporting two-sector ATPase


organism: Aphanothece halophytica

assay_conditions_summary: pH 7.6; cofactor ATP

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


substrate_name: Na+

substrate: Na+


organism: Acidaminococcus fermentans

substrate_name: reduced ferredoxin [iron-sulfur] cluster

proof_lines: at pH 6.8, temperature not specified in the publication


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

source_db: uniprot

protein_accession_database: UniProt

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

proof_lines: From other experiments a much lower Km for 5-methyl-5,6,7,8-tetrahydromethanopterin is estimated.

data_origin: experimental

source: uniprot


substrate_name: coenzyme M

substrate: coenzyme M


organism: Sus scrofa

proof_lines: in the presence of 0.00001 mM (3beta,22alpha,25R)-spirostan-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside

proof_lines: in the presence of 0.00001 mM (3beta,22alpha,25R)-26-(beta-D-glucopyranosyloxy)-2-methoxyfurost-5-en-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside


organism: Streptococcus gordonii


enzyme_display_name: ABC-type Cd(2+) transporter

organism: Saccharomyces cerevisiae

enzyme: ABC-type Cd(2+) transporter


substrate_name: leukotriene C4 [side 1]

substrate: leukotriene C4 [side 1]


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Pyrococcus furiosus

assay_conditions_summary: pH 6; 373.15 K; cofactor ATP


enzyme_display_name: H(+)-transporting two-sector ATPase

enzyme: H(+)-transporting two-sector ATPase


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

column_label: The abstract reports Vmax and Km values of approximately 0.8 s^-1 and 50+/-8 microM for basal Yor1p ATPase activity.

raw_value_unit_evidence: Km raw_value=50+/-8 microM raw_unit=microM

row_label: Prose segment: ATP Km

table_label: PubMed PMID 17950691 abstract


organism: Acetobacterium woodii

substrate_name: NAD+

assay_conditions_summary: pH 7.7; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: Na+/out

substrate: Na+/out


organism: Methanothermobacter marburgensis

substrate_name: CoM

substrate: CoM


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: ATP (in the presence of 150-153 mM of Na(+))


organism: Mycosarcoma maydis

substrate_name: K+

assay_conditions_summary: pH 6

substrate: K+


substrate_name: estradiol-beta-17-glucuronide [side 1]

verification_status: verified

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature S251A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor ATP

column_label: Table 3 row Ycf1p-S251A, column Km,app (uM), gives 187

raw_value_unit_evidence: Km,app (uM) = 187 uM

table_label: Table 3

substrate: estradiol-beta-17-glucuronide [side 1]

status: verified


sequence_source: UniProtKB P39109 FASTA

column_label: Table 3 row Ycf1p, column Km,app (uM), gives 394

raw_value_unit_evidence: Km,app (uM) = 394 uM


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature S251E to reconstruct the assayed variant sequence.

column_label: Table 3 row Ycf1p-S251E, column Km,app (uM), gives 481

raw_value_unit_evidence: Km,app (uM) = 481 uM


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature S908A/T911A to reconstruct the assayed variant sequence.

column_label: Table 3 row Ycf1p-S908A, T911A, column Km,app (uM), gives 548

raw_value_unit_evidence: Km,app (uM) = 548 uM


organism: Methanothermobacter thermautotrophicus


organism: Plasmodium falciparum

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: at pH 7.2, temperature not specified in the publication


organism: Bos taurus

assay_conditions_summary: pH 7


organism: Cereibacter sphaeroides

substrate_name: 2 horse heart ferricytochrome c1

substrate: 2 horse heart ferricytochrome c1


organism: Carcharhinus limbatus

substrate_name: ferrocytochrome c

substrate: ferrocytochrome c


organism: Alkalithermobacter thermoalcaliphilus

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: in the presence of Na+ at pH 7. 0 and 9.0


proof_lines:
horse heart cytochrome c
purified COV
unpurified COV


substrate_name: cytochrome c1

substrate: cytochrome c1


enzyme_display_name: magnesium chelatase

organism: Chlorobaculum tepidum

substrate_name: protoporphyrin IX

proof_lines: complex of subunits BchD, BchI, BchH3, pH 8.0, 34°C

proof_lines: complex of subunits BchD, BchI, BchH1, pH 8.0, 34°C

proof_lines: complex of subunits BchD, BchI, BchH2, pH 8.0, 34°C

enzyme: magnesium chelatase

substrate: protoporphyrin IX


enzyme_display_name: P-type H(+)-exporting transporter

organism: Coffea arabica

substrate_name: ATP

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines:
pH 6.5, 37°C, Colombia variety
pH 6.5, 37°C, Caturra variety

enzyme: P-type H(+)-exporting transporter


organism: Cyberlindnera jadinii

substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


organism: Crithidia fasciculata

proof_lines: Crithidia fasciculata cytochrome c, very low turnover numbers with human, yeast, rat, horse, and bovine cytochrome c


enzyme_display_name: Methylcobalamin:CoM methyltransferase isozyme A

organism: Methanosarcina acetivorans


enzyme: Methylcobalamin:CoM methyltransferase isozyme A


organism: Enterococcus hirae

substrate_name: Na+/in

proof_lines:
biphasic affinity
pH 8

substrate: Na+/in


enzyme_display_name: DNA ligase (ATP)

organism: Drosophila melanogaster

proof_lines:
p(dT)20 annealed with poly(dA)
DNA ligase I
DNA ligase II

enzyme: DNA ligase (ATP)

substrate: ATP


organism: Erythrobacter longus

substrate_name: ferrocytochrome c550

proof_lines:
Candida krusei cytochrome c
horse heart cytochrome c
horse cytochrome c as electron donor

substrate: ferrocytochrome c550


organism: Dictyostelium discoideum

proof_lines: 2 Km values for horse heart, Neurospora crassa, Saccharomyces cerevisiea and Candida krusei cytochrome c


enzyme_display_name: RNA 3'-terminal-phosphate cyclase (ATP)

organism: Escherichia coli

substrate_name: GTP

enzyme: RNA 3'-terminal-phosphate cyclase (ATP)

substrate: GTP


organism: Enterococcus faecalis


proof_lines: pH 7.5, 37°C, value of wild-type enzyme in comparison to values of mutant enzymes


substrate_name: Unknown

proof_lines: pH 8.0, 37°C, wild-type enzyme in comparison to mutant enzymes

substrate: Unknown


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D777N/Q1107R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D777N/V543I with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature D777N/N1027D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature D777N/S674L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature D777N/S1212L 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), so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature D777N/F565L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature D777N/A1003V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProt REST API Q08636


enzyme_display_name: ubiquinol oxidase (electrogenic, proton-motive force generating)

proof_lines:
presence of microcin J25, pH 6.4, 37°C
pH 6.4, 37°C


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, MgATPase activity of EcF1, in absence of selenite

proof_lines: pH 8.0, 37°C, MgATPase activity of EcF1, in presence of selenite


enzyme_display_name: DNA ligase (NAD(+))

substrate_name: nicked DNA

sequence_source: UniProt REST P25772

assay_conditions_summary: pH 7.8; 318.15 K; cofactor NAD+

enzyme: DNA ligase (NAD(+))

substrate: nicked DNA


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+


substrate_name: thio-NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: enzyme co-reconstituted with bacteriorhodopsin, in the dark

proof_lines: enzyme co-reconstituted with bacteriorhodopsin, in the light

substrate: thio-NADP+


enzyme_display_name: ubiquinol oxidase (H(+)-transporting)

enzyme: ubiquinol oxidase (H(+)-transporting)


enzyme_display_name: GMP synthase (glutamine-hydrolyzing)

enzyme: GMP synthase (glutamine-hydrolyzing)


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


mutation_signature: deletion mutant

mutation_type: deletion

assay_conditions_summary: cofactor ATP

proof_lines: deletion mutant, in comparison to the presence of effectors


organism: Galleria mellonella


organism: Euglena gracilis


organism: Gallus gallus


organism: eukaryota

assay_conditions_summary: pH 8

proof_lines: soluble enzyme, higher values for particulate enzyme


organism: Geobacillus stearothermophilus


organism: Haemophilus influenzae

proof_lines: pH and temperature not specified in the publication


organism: Homo sapiens

assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines: 30°C, in the presence of 0.0000125 mM replication protein A

proof_lines: at 30 mM Mg2+, pH and temperature not specified in the publication


enzyme_display_name: acetyl-CoA carboxylase

enzyme: acetyl-CoA carboxylase


organism: Haloferax volcanii

substrate_name: ADP

assay_conditions_summary: pH 9; 313.15 K; cofactor ATP

substrate: ADP


substrate_name: ATPgammaS

substrate: ATPgammaS


enzyme_display_name: NAD(+) synthase (glutamine-hydrolyzing)

enzyme: NAD(+) synthase (glutamine-hydrolyzing)


sequence_variant_note: Resolved canonical sequence from uniprot_rest:P39109 and applied mutation signature D777N/G1207D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest:P39109 and applied mutation signature D777N/G1207S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest:P39109 and applied mutation signature D777N/A1021T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest:P39109 and applied mutation signature D777N/R1415G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest:P39109 and applied mutation signature D777N/A1021V to reconstruct the assayed variant sequence.


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


enzyme_display_name: methylcrotonoyl-CoA carboxylase

organism: Hordeum vulgare

substrate_name: bicarbonate

assay_conditions_summary: cofactor CoA

enzyme: methylcrotonoyl-CoA carboxylase

substrate: bicarbonate


enzyme_display_name: cytochrome-c oxidase

proof_lines:
high-affinity reaction
low-affinity reaction
high-affinity Km

enzyme: cytochrome-c oxidase


assay_conditions_summary: pH 8.5; 305.15 K; cofactor ATP


organism: Klebsiella pneumoniae


organism: Lathyrus oleraceus

assay_conditions_summary: pH 6.5; cofactor ATP

proof_lines: presence of 5 mM methyl-beta-cyclodextrin, pH 6.5, temperature not specified in the publication

proof_lines: presence of 15 mM methyl-beta-cyclodextrin, pH 6.5, temperature not specified in the publication

proof_lines: presence of 2 mM methyl-beta-cyclodextrin, pH 6.5, temperature not specified in the publication


organism: Mus musculus

substrate_name: ferricytochrome c

assay_conditions_summary: cofactor NADH

proof_lines:
in the presence of 0.1 mM daunorubicin
in the presence of 0.1 mM mitoxantrone
in the presence of 0.1 mM ametantrone

substrate: ferricytochrome c


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: pH 7.0, 30°C, N-terminally tagged protein


organism: Methanothermobacter thermautotrophicus

proof_lines: 37°C, pH not specified in the publication, in the presence of bovine serum albumin (0.002 mM)


proof_lines:
following sham exposure
following CO exposure


organism: Mycobacterium tuberculosis


substrate: NAD+


enzyme_display_name: quinol--cytochrome-c reductase

organism: Neurospora crassa

enzyme: quinol--cytochrome-c reductase


organism: Leptolyngbya foveolarum


organism: Nitrobacter winogradskyi

proof_lines:
horse cytochrome c
cow cytochrome c
Saccharomyces oviformis cytochrome c


organism: Oryctolagus cuniculus

substrate_name: ferricytochrome b5

proof_lines: long ferricytochrome b5 from pig microsomes, at pH 6.5 and 30°C

proof_lines: long ferricytochrome b5 from rat microsomes, at pH 6.5 and 30°C

proof_lines: long ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C

substrate: ferricytochrome b5


organism: Oryza sativa

proof_lines: enzyme purified from plants exposed to simulated acid rain, pH not specified in the publication, temperature not specified in the publication

proof_lines: enzyme purified from control plants, pH not specified in the publication, temperature not specified in the publication


organism: Paracoccus denitrificans

substrate_name: 2 ferricytochrome c

substrate: 2 ferricytochrome c


organism: Ovis aries

substrate_name: ferrocytochrome c

proof_lines: enzyme from swayback-diseased liver, low-affinity Km

proof_lines: enzyme from swayback-diseased brain, low-affinity Km

proof_lines: enzyme from normal liver, high-affinity Km

substrate: ferrocytochrome c


organism: Nitrosomonas europaea

proof_lines:
horse cytochrome c
Candida krusei cytochrome c
Nitrosomonaseuropaea cytochrome c


proof_lines: horse heart cytochrome c, chymotrypsin treated enzyme


organism: Phycomyces blakesleeanus


organism: Populus euphratica


organism: Pseudomonas sp.

proof_lines:
Candida krusei cytochrome c
horse and native cytochrome c


organism: Priestia megaterium

proof_lines:
strain NRLL B939
strain KM


organism: Homo sapiens

proof_lines:
pH 7.5, recombinant enzyme
at 37°C


substrate_name: Cu(II)-nitrilotriacetic acid[side 2]

proof_lines: in 25 mM MOPS, 25 mM MES, 5.4 mM KCl, 5 mM glucose, 140 mM NaCl, 1.8 mM CaCl2, 0.8 mM MgCl2, pH 7.0, at 22°C

proof_lines: in 25 mM MOPS, 25 mM MES, 5.4 mM KCl, 5 mM glucose, 140 mM NaCl, 1.8 mM CaCl2, 0.8 mM MgCl2, pH 7.0, at 37°C

substrate: Cu(II)-nitrilotriacetic acid[side 2]


organism: Rattus norvegicus

substrate_name: ATP


organism: Pseudoalteromonas haloplanktis


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: L-ascorbate

substrate: L-ascorbate


substrate_name: L-Gln

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

substrate: L-Gln


substrate_name: L-Asp

substrate: L-Asp


enzyme_display_name: 3'-phosphate/5'-hydroxy nucleic acid ligase

organism: Pyrococcus horikoshii

proof_lines: pH 7.0, 70°C, presence of archease, ligation reaction


proof_lines: short ferricytochrome b5 from rat microsomes, at pH 6.5 and 30°C

proof_lines: short ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C


substrate: ATP


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: in presence of 10 mM ATP plus 15 mM MgCl2


proof_lines:
fetal heart enzyme
adult heart enzyme


proof_lines:
DNA ligase II
DNA ligase I


assay_conditions_summary: 310.15 K; cofactor CoA

proof_lines:
hindlimb muscle
adipose tissue
at 37°C


substrate_name: acetyl-CoA

proof_lines:
at 37°C
adipose tissue
hindlimb muscle

substrate: acetyl-CoA


enzyme_display_name: pyruvate carboxylase

organism: Rhizobium etli

substrate_name: Unknown

enzyme: pyruvate carboxylase

substrate: Unknown


substrate_name: oxamate

proof_lines: ATPase reaction, wild-type, pH 7.5, 25°C

proof_lines: wild type enzyme, in 100 mM Tris-HCl pH 7.8, 30°C

substrate: oxamate


substrate_name: oxaloacetate

proof_lines:
pH 7.5, 25°C, 0.25 mM oxamate
pH 7.5, 25°C, 0.5 mM oxamate
pH 7.5, 25°C, 0.75 mM oxamate

substrate: oxaloacetate


organism: Rhizoprionodon terraenovae

proof_lines:
heart enzyme
muscle enzyme


substrate_name: pyruvate

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

proof_lines: hybrid tetramers between mutants K1119Q and R472S, pH 7.8, 30°C

substrate: pyruvate


organism: Rhodobacter capsulatus

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: coenzyme Q1H2

proof_lines: estimated value of KM, descriptive of rotenone-dicumarol-insensitive CoQ1 reduction and CoQ1H2 oxidation on passage through normoxic lungs

substrate: coenzyme Q1H2


assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: presence of 2' -3' -O-(2,4,6-trinitrophenyl) adenosine 5' -diphosphate, pH 7.8, 30°C

proof_lines: presence of 2' -3' -O-(2,4,6-trinitrophenyl) adenosine 5' -phosphate, pH 7.8, 30°C


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


enzyme_display_name: ABC-type Cd(2+) transporter

organism: Saccharomyces cerevisiae

substrate_name: bilirubin

proof_lines:
in vesicles
in vacuoles

substrate: bilirubin


substrate_name: 2 ferricytochrome c1

substrate: 2 ferricytochrome c1


organism: Rhodopseudomonas palustris

substrate_name: ferrocytochrome c

proof_lines: oxidation of bovine or yeast cytochrome c

substrate: ferrocytochrome c


substrate_name: ubiquinol

substrate: ubiquinol


proof_lines:
pH 8.0, 23°C
purified enzyme
pH 7.0, 22°C


organism: Rhodospirillum rubrum

substrate_name: oxidized 3-acetylpyridine adenine dinucleotide

proof_lines: kcat for recombinant domain III in the presence of saturating amounts of domain I, reduction of acetylpyridine adenine dinucleotide by NADPH

proof_lines: kcat for recombinant domain I in the presence of saturating amounts of domain III, reduction of acetylpyridine adenine dinucleotide by NADPH


substrate_name: decylubiquinol

proof_lines: different purified enzyme preparations, in 0.01% Tween 20, 250 mM sucrose

substrate: decylubiquinol


proof_lines: horse heart cytochrome c, high-affinity Km, 30 mM ionic strength

proof_lines: horse heart cytochrome c, 100 mM ionic strength


enzyme_display_name: adenosylcobyric acid synthase (glutamine-hydrolyzing)

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: adenosylcobyrinic acid triamide

substrate: adenosylcobyrinic acid triamide


substrate_name: cytochrome c1

substrate: cytochrome c1


enzyme_display_name: P-type H(+)-exporting transporter

organism: Schizosaccharomyces pombe

substrate_name: ATP


organism: Sphyrna lewini


enzyme_display_name: H(+)-transporting two-sector ATPase

organism: Spinacia oleracea

assay_conditions_summary: buffer 2-(N-morpholino)ethane sulfonic acid buffer; cofactor ATP


assay_conditions_summary: pH 7

proof_lines:
pH 7.0, wild-type enzyme
pH 8.0, wild-type enzyme


organism: Staphylococcus aureus


enzyme_display_name: H(+)-exporting diphosphatase

organism: Sesamum indicum

substrate_name: diphosphate

enzyme: H(+)-exporting diphosphatase

substrate: diphosphate


organism: Stutzerimonas stutzeri


organism: Sus scrofa

substrate_name: Unknown

proof_lines: noncompetitive versus cytochrome c, pH 7.4, 23°C

proof_lines: competitive versus decylubiquinol, pH 7.4, 23°C


proof_lines: enzyme from diaphragm, photometric assay


enzyme_display_name: protein-secreting ATPase

organism: Shigella flexneri

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

enzyme: protein-secreting ATPase

substrate: ATP


organism: Streptomyces sp.

substrate_name: L-Asp

substrate: L-Asp


assay_conditions_summary: pH 9; cofactor ATP

proof_lines: presence of Mn2+, pH 9.0, temperature not specified in the publication

proof_lines: presence of Mg2+, pH 9.0, temperature not specified in the publication

proof_lines: presence of Ca2+, pH 9.0, temperature not specified in the publication

enzyme: H(+)-transporting two-sector ATPase


organism: Thermus scotoductus

substrate_name: nicked DNA

substrate: nicked DNA


substrate_name: ferricytochrome b5

proof_lines: short ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C

proof_lines: long ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C

proof_lines: short ferricytochrome b5 from pig microsomes, at pH 6.5 and 30°C

substrate: ferricytochrome b5


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

enzyme: ABC-type Cd(2+) transporter

substrate: glutathione


organism: Squalus acanthias


enzyme_display_name: plastoquinol--plastocyanin reductase

organism: Trichormus variabilis

enzyme: plastoquinol--plastocyanin reductase


organism: Triticum aestivum

proof_lines: biphasic kinetic, high-affinity phase Km


organism: Vibrio harveyi

proof_lines: at 30°C, 100 mM KCl, 20 mM HEPES/Tris (pH 7.5)

substrate: Unknown


organism: Thermus thermophilus

proof_lines:
horse cytochrome c
Candida krusei cytochrome c
Thermus thermophilus cytochrome c


substrate_name: NADH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

substrate: NADH


organism: Zea mays

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


smiles: N


organism: Homo sapiens

substrate_name: H2O; L-Glutamine; ATP; Deamino-NAD+

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

substrate: H2O; L-Glutamine; ATP; Deamino-NAD+


organism: Mustela vison

substrate_name: Hydrogencarbonate; Pyruvate; ATP

assay_conditions_summary: cofactor ATP

substrate: Hydrogencarbonate; Pyruvate; ATP


organism: Bacillus megaterium

substrate_name: ATP; H2O

substrate: ATP; H2O


organism: Thermobifida fusca

enzyme: 3'-phosphate/5'-hydroxy nucleic acid ligase


proof_lines:
pH 7.4, 70°C
pH 7.4, 70°C, presence of archease


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
cytosolic enzyme, pH 8.0, 30°C
non-mesophyll chloroplast isoform
plastidic enzyme, pH 8.0, 30°C


organism: Enterococcus faecium

substrate_name: H2O; ATP

substrate: H2O; ATP


organism: Geobacillus stearothermophilus

substrate_name: Hydrogencarbonate; L-Glutamine; H2O; ATP


organism: Saccharomyces cerevisiae

substrate_name: H2O; ATP; H+

substrate: H2O; ATP; H+


organism: Alopecurus myosuroides

substrate_name: Hydrogencarbonate; Acetyl-CoA; ATP

substrate: Hydrogencarbonate; Acetyl-CoA; ATP


organism: Lactobacillus casei


organism: Lactococcus lactis


organism: Streptococcus salivarius


organism: Festuca rubra

substrate_name: ATP; Acetyl-CoA; Hydrogencarbonate

substrate: ATP; Acetyl-CoA; Hydrogencarbonate


organism: Solanum tuberosum


organism: Streptococcus milleri


substrate_name: Hydrogencarbonate; ATP; Acetyl-CoA

substrate: Hydrogencarbonate; ATP; Acetyl-CoA


enzyme_display_name: P-type Zn(2+) transporter

organism: Homarus americanus

proof_lines: pH condition outward gradient, pH = 5.0/7.0

proof_lines: carrier transport is stimulated by the addition of 1 mM ATP

enzyme: P-type Zn(2+) transporter


enzyme_display_name: P-type Ca(2+) transporter

organism: Sepioteuthis sepioidea

enzyme: P-type Ca(2+) transporter


substrate_name: ATP


enzyme_display_name: Na(+)/K(+)-exchanging ATPase

organism: Callinectes danae

substrate_name: K+

proof_lines: apparent dissociation constant in the presence of 2 mM spermidine

enzyme: Na(+)/K(+)-exchanging ATPase

substrate: K+


substrate_name: Na+

substrate: Na+


organism: Clibanarius vittatus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: low-affinity ATP hydrolyzing site, 25°C, pH 7.5

substrate: ATP


substrate_name: Unknown

proof_lines:
25°C, pH 7.5
at pH 7.5 and 25°C


organism: Cardisoma guanhumi


organism: Rattus norvegicus

substrate_name: K+; Na+; H2O; ATP

substrate: K+; Na+; H2O; ATP


substrate_name: ATP; Na+; K+; H2O

substrate: ATP; Na+; K+; H2O


substrate_name: Na+; H2O; ATP; K+

substrate: Na+; H2O; ATP; K+


substrate_name: K+; Na+; ATP; H2O

substrate: K+; Na+; ATP; H2O


organism: Xiphopenaeus kroyeri

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP


substrate: Unknown


organism: Homo sapiens

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: ATPase turnover rate, pH 7.0, 37°C, isozyme SPCA1a

proof_lines: ATPase turnover rate, pH 7.0, 37°C, isozyme SPCA1d

proof_lines: ATPase turnover rate, pH 7.0, 37°C, isozyme SPCA1b


organism: Melanogrammus aeglefinus

substrate_name: H2O; ATP; Ca2+

substrate: H2O; ATP; Ca2+


enzyme_display_name: P-type Mg(2+) transporter

organism: Cytobacillus firmus

enzyme: P-type Mg(2+) transporter


proof_lines:
pH 7.4, 37°C, MgtE
pH 7.4, 37°C, MgtE, above


organism: Mytilus galloprovincialis

assay_conditions_summary: pH 9; 303.15 K; cofactor ATP

proof_lines:
pH 9.0, 30°C, gill enzyme
pH 9.0, 30°C, mantle enzyme


proof_lines:
pH 9.0, 30°C, mantle enzyme
pH 9.0, 30°C, gill enzymem


organism: uncultured bacterium

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: in the presence of 5 mM Mg2+, at pH 7.2 and 37°C


enzyme_display_name: ABC-type Ni(2+) transporter

organism: Thermoanaerobacter kivui

enzyme: ABC-type Ni(2+) transporter


organism: Macrobrachium amazonicum

proof_lines:
salinity-acclimated shrimp
freshwater shrimp
at pH 7.5 and 25°C


enzyme_display_name: P-type Cu(2+) transporter

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ATP

enzyme: P-type Cu(2+) transporter


organism: Goniopsis cruentata


organism: Macrobrachium rosenbergii


organism: Pareledone sp.

substrate_name: Na+/in

proof_lines: maximum turnover rate per pump, pH not specified in the publication, 22°C

substrate: Na+/in


organism: Amatitlania nigrofasciata

substrate_name: Ca2+; H2O; ATP

substrate: Ca2+; H2O; ATP


enzyme_display_name: Cd(2+)-exporting ATPase

organism: Oncorhynchus mykiss

proof_lines: in the presence of 2.5 mM Fe2+, pH and temperature not specified in the publication

proof_lines: in the presence of 0.01 mM Zn2+, pH and temperature not specified in the publication

enzyme: Cd(2+)-exporting ATPase


enzyme_display_name: P-type Ag(+) transporter

substrate_name: Ag+

enzyme: P-type Ag(+) transporter

substrate: Ag+


organism: Oryctolagus cuniculus

proof_lines: predicted, in the presence of 5.6 mM external K+

proof_lines: predicted, in the presence of 15 mM external K+


enzyme_display_name: H(+)/K(+)-exchanging ATPase

organism: Necturus maculosus

enzyme: H(+)/K(+)-exchanging ATPase


substrate_name: ATP; H2O; Ca2+

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

substrate: ATP; H2O; Ca2+


substrate_name: Ca2+; ATP; H2O

substrate: Ca2+; ATP; H2O


substrate_name: ATP; Ca2+; H2O

substrate: ATP; Ca2+; H2O


organism: Escherichia coli

substrate_name: H2O; Zn2+; ATP

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

substrate: H2O; Zn2+; ATP


organism: Enterococcus hirae

substrate_name: H2O; ATP; Ag+

substrate: H2O; ATP; Ag+


organism: Escherichia coli (strain K12)

substrate_name: Pb(2+)-thiolate (at 37 degrees Celsius and pH 7.0)


enzyme_display_name: P-type Cu(+) transporter

organism: Archaeoglobus fulgidus

substrate_name: ATP

sequence_source: multiple

assay_conditions_summary: pH 6.1; cofactor ATP

proof_lines: Shows higher affinity for Cu(+) compared with Ag(+).

source_databases_merged: brenda uniprot

enzyme: P-type Cu(+) transporter


enzyme_display_name: P-type K(+) transporter

organism: Bacillus subtilis

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

enzyme: P-type K(+) transporter


organism: Homo sapiens


organism: Myroides odoratus


organism: Callinectes sapidus

proof_lines: posterior gill, juvenile crab acclimated to dilute seawater of 150 mOsm, pH 7.4

proof_lines: anterior gill, sub-adult crab acclimated to dilute seawater of 150 mOsm, pH 7.4


organism: Electrophorus electricus

substrate_name: K+/out

proof_lines: enzyme from main electric organ, at pH 7.2 and 25°C

proof_lines: enzyme from Sach's electric organ, at pH 7.2 and 25°C

proof_lines: enzyme from Hunter's electric organ, at pH 7.2 and 25°C

substrate: K+/out


organism: Octopus bimaculatus


enzyme_display_name: ABC-type ferric hydroxamate transporter

substrate_name: Unknown

enzyme: ABC-type ferric hydroxamate transporter


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D824A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D824E with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E820D with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P810G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I940A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F818C with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T823V with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature I819L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T929L with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature P810A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L811V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L811F to reconstruct the assayed variant sequence.


substrate_name: ATP; H2O; K+

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

substrate: ATP; H2O; K+


substrate_name: K+; ATP; H2O

substrate: K+; ATP; H2O


substrate_name: Cu+; ATP; H2O

substrate: Cu+; ATP; H2O


substrate_name: ATP; Cu+; H2O

substrate: ATP; Cu+; H2O


organism: Thermotoga maritima

substrate_name: Cu+[side 1]

substrate: Cu+[side 1]


proof_lines: Export tested with Isoform Copper-exporting P-type ATPase.


substrate_name: copper

smiles: [Cu]

substrate: copper


substrate: ATP


assay_conditions_summary: pH 6.1; 348.15 K; cofactor ATP

source_databases_merged: sabio_rk brenda uniprot


organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

substrate_name: ATP in conformational state E1 (at 37 degrees Celsius)

proof_lines: kcat is 248 min(-1) for the ATPase activity.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y799F to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature P798C with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y925A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature F917Y with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y925F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E914Q with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Cavia porcellus

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

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: pH 7.4, temperature not specified in the publication, with optimal concentration of ATP, Mg2+ and K+

proof_lines: pH 7.0, temperature not specified in the publication, with optimal concentration of ATP, Mg2+ and K+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q905N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I803L to reconstruct the assayed variant sequence.


organism: Sus scrofa


substrate_name: K+[side 2]

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E343Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: K+[side 2]


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E795Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines:
wild type enzyme, at pH 7.0 and 37°C
wild type enzyme, at pH 7.6 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C27A/C30A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP


substrate_name: Pb(2+) (at 37 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7


substrate_name: Zn(2+) (at 37 degrees Celsius and pH 7.0)


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

substrate_name: magnesium ions (at 37 degrees Celsius)

substrate: magnesium ions (at 37 degrees Celsius)


substrate_name: magnesium ions (at 20 degrees Celsius)

substrate: magnesium ions (at 20 degrees Celsius)


substrate_name: calcium (at 8 degrees Celsius)

smiles: [Ca]

column_label: PubMed abstract metric sentence gives Km for calcium as 1.5 microM, normalized to 0.0015 mM

normalized_value_unit_evidence: PubMed abstract Km normalized_value=0.0015 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: The purified Ca2+-ATPase has an apparent Km for calcium of 1.5 microM and for ATP of 90 microM

row_label: Ca2+-ATPase calcium Km sentence

table_label: PubMed abstract

substrate: calcium (at 8 degrees Celsius)


substrate_name: ATP (at 8 degrees Celsius)

substrate: ATP (at 8 degrees Celsius)


substrate: Pb(2+) (at 37 degrees Celsius and pH 7.0)


substrate: Zn(2+) (at 37 degrees Celsius and pH 7.0)


substrate_name: Cd(2+) (at 37 degrees Celsius and pH 7.0)


substrate_name: Cu(2+) (at 37 degrees Celsius and pH 7.0)


substrate_name: Ni(2+) (at 37 degrees Celsius and pH 7.0)


substrate_name: Co(2+) (at 37 degrees Celsius and pH 7.0)


organism: Cereibacter sphaeroides

substrate_name: K+

substrate: K+


substrate: Cd(2+) (at 37 degrees Celsius and pH 7.0)


substrate: Cu(2+) (at 37 degrees Celsius and pH 7.0)


substrate: Ni(2+) (at 37 degrees Celsius and pH 7.0)


substrate: Co(2+) (at 37 degrees Celsius and pH 7.0)


substrate_name: ATP (ATPase activity)

assay_conditions_summary: pH 1

substrate: ATP (ATPase activity)


organism: Noccaea caerulescens

substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: in the presence of Zn2+ or Cd2+, in 0.6 M Tris, 2 M NaCl and 0.1 M MgCl2, pH 8.0, at 30°C


substrate_name: ATP (in complex with NPTN)

substrate: ATP (in complex with NPTN)


substrate_name: ATP using FhuCB complex

substrate: ATP using FhuCB complex


organism: Escherichia coli

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

proof_lines:
mutant C392S
+ thiolate, mutant C392S


proof_lines:
mutant C392H
+ thiolate, mutant C392H


proof_lines:
mutant C394H
+ thiolate, mutant C394H


proof_lines:
mutant C392H/C394H
+ thiolate, mutant C392H/C394H


proof_lines:
mutant C392S/C394S
+ thiolate, mutant C392S/C394S


proof_lines:
mutant C394S
+ thiolate, mutant C394S


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

proof_lines:
wild-type ZntA
+ thiolate, wild-type ZntA


organism: Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R)

assay_conditions_summary: pH 6.25; cofactor ATP

column_label: Abstract reports purified CopA catalyzed ATP hydrolysis with Vmax 0.15 micromol/min/mg and a Km for ATP of 0.2 mM.

raw_value_unit_evidence: Km raw_value=0.2 mM raw_unit=mM

row_label: Enterococcus hirae CopA / ATP hydrolysis

table_label: PubMed XML abstract PMID 11162579

substrate: ATP


proof_lines: pH 7.0, 37°C, mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC


proof_lines:
pH 7.0, 37°C, enzyme
pH 7.0, 37°C


substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


proof_lines:
pH 7.0, 37°C
pH 7.0, 37°C, enzyme


organism: Oryctolagus cuniculus

substrate_name: Unknown

substrate: Unknown


proof_lines: pH 7.4, 37°C, mutant enzyme G918E and mutant enzyme Y922I


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
pH 7.4, 37°C, MgtB
pH 7.4, 37°C, MgtA
pH 7.4, 37°C, CorA


proof_lines:
pH 7.4, 37°C, MgtA
pH 7.4, 37°C, MgtB
pH 7.4, 37°C, CorA


organism: Alicyclobacillus acidocaldarius


assay_conditions_summary: cofactor ATP


organism: Canis lupus familiaris


substrate_name: Cu+

proof_lines: apparent Km-value of C14A/C17A/C110A/C113A mutant protein, pH 6.8, 20°C

substrate: Cu+


proof_lines: apparent Km-value of wild-type protein, pH 6.8, 20°C


assay_conditions_summary: pH 6.8; 293.15 K; cofactor ATP


substrate_name: Pb2+[side 1]

substrate: Pb2+[side 1]


substrate_name: Cd2+[side 1]

substrate: Cd2+[side 1]


organism: Homo sapiens

proof_lines: pH 7.0, 37°C, recombinant enzyme, in presence of 100 mM Na+

proof_lines: pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM NH4+

proof_lines: pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM K+


organism: Rattus norvegicus

proof_lines: red gastrocnemius, total membranes, after exercise (running)


substrate_name: Na+

proof_lines:
red gastrocnemius, total membranes
soleus, total membranes
oxidative fiber, sarcolemmal membrane

substrate: Na+


proof_lines: wild-type enzyme in absence of detergent


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

proof_lines: mutant D813A/D818A in absence of detergent


organism: Aplysia californica

substrate_name: Ca2+[side 1]

proof_lines: pH and temperature not specified in the publication

substrate: Ca2+[side 1]


proof_lines: isoform 3c in presence of a saturing Ca2+ at pH 7.0, in presence of ionophore

proof_lines: isoform 3a in presence of a saturing Ca2+ concentration at pH 7.0, in presence of ionophore

proof_lines: isoform 3b in presence of a saturing Ca2+ at pH 7.0, in presence of ionophore


substrate_name: H2O; Na+; ATP; K+

proof_lines: pH 7.4, 37°C, Na/K-ATPase-enriched A-127 cell extract

substrate: H2O; Na+; ATP; K+


substrate_name: UTP

substrate: UTP


enzyme_display_name: ABC-type Fe(3+) transporter

organism: Haemophilus influenzae

enzyme: ABC-type Fe(3+) transporter


proof_lines: in the presence of 4 mM Mg2+, at pH 7.2 and 37°C


substrate_name: Mg2+[side 1]

proof_lines:
with 3 or 6 mM ATP, at pH 7.0 and 37°C
with 1 mM ATP, at pH 7.0 and 37°C

substrate: Mg2+[side 1]


organism: Mycobacterium tuberculosis

substrate_name: Cu+[side 1]

substrate: Cu+[side 1]


proof_lines: in presence of 0.1 mM Ca2+ at pH optimum 7.23, in presence of ionophore

proof_lines: in presence of a saturing Ca2+ at pH 7.0, in presence of ionophore


organism: Paramecium tetraurelia


proof_lines: pH 7.2, 37°C, enzyme from medial pterygoid muscles

proof_lines: pH 7.2, 37°C, enzyme from masseter muscles


substrate_name: Na+/in

proof_lines:
alpha1beta1 heterodimer, 37°C, pH 7.4
alpha2beta1 heterodimer, 37°C, pH 7.4
alpha1beta2 heterodimer, 37°C, pH 7.4

substrate: Na+/in


proof_lines: SERCA from undifferentiated or differentiated PC-12 cells


proof_lines:
MgtB
pH 7.4, 37°C, MgtB
pH 7.4, 37°C, CorA


organism: Mus musculus


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines:
pH 7.4, 37°C, control
pH 7.4, 37°C, neonatal hypothyroidism
pH 7.4


organism: Schistosoma mansoni


organism: Sus scrofa

proof_lines: Km1 value, plus gamma subunit, pH 7.4, 37°C


organism: Salmo salar

substrate_name: ATP; H2O; Ca2+

substrate: ATP; H2O; Ca2+


organism: Mesocricetus auratus

substrate_name: K+

substrate: K+


organism: Oncorhynchus mykiss

substrate_name: ATP; Ca2+; H2O

substrate: ATP; Ca2+; H2O


organism: Trypanosoma equiperdum

proof_lines: in the presence of 0.008 mg/ml calmodulin, at pH 7.2 and 37°C

proof_lines: in the absence of calmodulin, at pH 7.2 and 37°C


enzyme_display_name: ABC-type phosphate transporter

organism: Arabidopsis thaliana

substrate_name: phosphate/out

proof_lines: pH and temperature not specified in the publication

enzyme: ABC-type phosphate transporter

substrate: phosphate/out


organism: Saccharomyces cerevisiae

substrate_name: ATP

mutation_signature: Δ1

proof_lines: mutant lacking N-terminal SPX domain DELTA1-375, pH and temperature not specified in the publication

substrate: ATP


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


substrate_name: phosphate

substrate: phosphate


organism: Chrysanthemum x morifolium


enzyme_display_name: glutaconyl-CoA decarboxylase

organism: Pseudomonas sp.

substrate_name: glutaryl-CoA

assay_conditions_summary: pH 7.5; 301.15 K; cofactor CoA

enzyme: glutaconyl-CoA decarboxylase

substrate: glutaryl-CoA


substrate_name: glutaconyl-CoA

substrate: glutaconyl-CoA


organism: Medicago truncatula


proof_lines: Vmax: 134 nmol/min/mg protein, pH 7, 27°C


organism: Hordeum vulgare

proof_lines: pH 7.5, temperature not specified in the publication

proof_lines: isozyme HvPHT1;1, pH and temperature not specified in the publication

proof_lines: isozyme HvPHT1;6, pH and temperature not specified in the publication


proof_lines: pH 6.0, 30°C, Vmax: 860 pmol of phosphate incorporated per min/OD650


proof_lines: wild-type, pH 6.0, 30°C, Vmax: 440 pmol of phosphate incorporated per min/OD650


proof_lines: using triple mutant DELTApho87-DELTApho90-DELTApho91, pH 6.0, 30°C, Vmax: 2000 pmol of phosphate incorporated per min/OD650


substrate_name: Unknown

substrate: Unknown


proof_lines: using triple mutant DELTApho87-DELTApho90-DELTApho91


organism: Acidaminococcus fermentans

substrate_name: Glutaconyl-1-CoA; CO2; Crotonoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: Glutaconyl-1-CoA; CO2; Crotonoyl-CoA


substrate_name: Na+

substrate: Na+


substrate_name: Glutaconyl-1-CoA; Crotonoyl-CoA; CO2

substrate: Glutaconyl-1-CoA; Crotonoyl-CoA; CO2


enzyme_display_name: Na(+)-exporting diphosphatase

organism: Thermotoga maritima

substrate_name: diphosphate

proof_lines: 40°C, pH 7.2, active site 1, presence of 5 mM MgCl2

proof_lines: 40°C, pH 7.2, active site 1, presence of 1 mM MgCl2

proof_lines: 40°C, pH 7.2, active site 2, presence of 1 mM MgCl2

enzyme: Na(+)-exporting diphosphatase

substrate: diphosphate


organism: Solanum lycopersicum

proof_lines: isozyme OsPT8, pH and temperature not specified in the publication

proof_lines: isozyme OsPT6, pH and temperature not specified in the publication


organism: Sinorhizobium meliloti


enzyme_display_name: ABC-type polar-amino-acid transporter

substrate_name: glycine/out

proof_lines: Gap mutant K9R,K16R/A297V, pH and temperature not specified in the publication

enzyme: ABC-type polar-amino-acid transporter

substrate: glycine/out


proof_lines: Gap mutant K9R,K16R, pH and temperature not specified in the publication


enzyme_display_name: ABC-type sulfate transporter

organism: Alicyclobacillus acidocaldarius

assay_conditions_summary: 333.15 K; cofactor ATP

enzyme: ABC-type sulfate transporter


organism: Oryza sativa

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: ABC-type nitrate transporter

organism: Marinomonas mediterranea

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

enzyme: ABC-type nitrate transporter


enzyme_display_name: ABC-type molybdate transporter

substrate_name: molybdate

enzyme: ABC-type molybdate transporter

substrate: molybdate


organism: Bradyrhizobium japonicum


organism: Clostridium pasteurianum


substrate_name: nitrate/out

substrate: nitrate/out


proof_lines: mutant S124A, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 47 nmol/mg of protein/h

proof_lines: mutant S124A, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 62 nmol/mg of protein/h


proof_lines: mutant D382E, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 96 nmol/mg of protein/h

proof_lines: mutant D382E, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 132 nmol/mg of protein/h


proof_lines: mutant D382A, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 156 nmol/mg of protein/h

proof_lines: mutant D382A, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 119 nmol/mg of protein/h


proof_lines: wild-type, pH 6.5, 25°C, in the presence of 25 mM NaCl

proof_lines: wild-type, pH 6.5, 25°C, in the presence of various concentrations of NaCl


proof_lines: mutant R228K, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 274 nmol/mg of protein/h

proof_lines: mutant R228K, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 221 nmol/mg of protein/h


proof_lines: mutant S124T, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 254 nmol/mg of protein/h

proof_lines: mutant S124T, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 222 nmol/mg of protein/h


proof_lines: mutant R120K, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 250 nmol/mg of protein/h

proof_lines: mutant R120K, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 125 nmol/mg of protein/h


proof_lines: mutant R201K, pH 6.5, 25°C, in the presence of 25 mM NaCl, Vmax (adjusted to the protein expression levels): 100.7 nmol/mg of protein/h

proof_lines: mutant R201K, pH 6.5, 25°C, in the presence of various concentrations of NaCl, Vmax (adjusted to the protein expression levels): 126 nmol/mg of protein/h


organism: Citrullus lanatus

proof_lines: isoform AAP3, whole cell import assay in transgenic yeast, pH not specified in the publication, temperature not specified in the publication

proof_lines: isoform AAP6, whole cell import assay in transgenic yeast, pH not specified in the publication, temperature not specified in the publication


organism: Picosynechococcus sp. PCC 7002

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


organism: Oryza sativa Japonica Group

proof_lines: whole cell import assay in transgenic yeast, pH not specified in the publication, 30°C


organism: Penicillium chrysogenum

substrate_name: alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]


organism: Rhizobium leguminosarum

substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-glutamate

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

substrate: L-glutamate


substrate_name: L-alanine

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

substrate: L-alanine


substrate_name: L-leucine

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

substrate: L-leucine


substrate_name: alpha-aminoisobutyric acid

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

substrate: alpha-aminoisobutyric acid


organism: Hebeloma cylindrosporum


organism: Bacillus subtilis

proof_lines: BcaP, at 26°C, pH not specified in the publication

proof_lines: BraB, at 26°C, pH not specified in the publication


substrate: alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]


organism: Pinus pinaster

proof_lines: whole cell import assay in transgenic yeast, pH not specified in the publication, temperature not specified in the publication


organism: Homo sapiens

substrate_name: ATP

sequence_variant_note: Mutation signature W653Y references residue 653, which is outside the resolved sequence length.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP


sequence_variant_note: Mutation signature Y1302W references residue 1302, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W653Y/Y1302W references residue 653, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W653C/Y1302W references residue 653, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W653C references residue 653, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature Y1302C references residue 1302, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W653Y/Y1302C references residue 653, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W653C/Y1302C references residue 653, which is outside the resolved sequence length.


organism: Leishmania donovani

substrate_name: L-lysine/out

substrate: L-lysine/out


organism: Staphylococcus aureus

proof_lines: isoform BrnQ1, at 37°C, pH not specified in the publication

proof_lines: isoform BrnQ2, at 37°C, pH not specified in the publication


organism: Mycobacterium tuberculosis

substrate_name: sulfate

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

assay_conditions_summary: pH 6

substrate: sulfate


enzyme_display_name: P-type Mn(2+) transporter

substrate_name: Mn2+; ATP; H2O

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

enzyme: P-type Mn(2+) transporter

substrate: Mn2+; ATP; H2O


organism: Acetobacterium woodii

substrate_name: Na+[side 1]

substrate: Na+[side 1]


organism: Arabidopsis thaliana

substrate_name: ATP; Phosphate; H2O

substrate: ATP; Phosphate; H2O


organism: Acyrthosiphon pisum


substrate_name: ATP; H2O; L-Aspartate

substrate: ATP; H2O; L-Aspartate


substrate_name: H2O; L-Aspartate; ATP

substrate: H2O; L-Aspartate; ATP


organism: Saccharomyces cerevisiae

substrate_name: Unknown

substrate: Unknown


substrate_name: L-Aspartate; H2O; ATP

substrate: L-Aspartate; H2O; ATP


substrate_name: L-glutamine/out

proof_lines: wild-type LHT1, pH 5.8, temperature not specified in the publication

substrate: L-glutamine/out


proof_lines: glutamateex/glutaminein antiport, pH 7, temperature not specified in the publication

proof_lines: glutamateex/glutaminein antiport, pH 6, temperature not specified in the publication

proof_lines: glutamateex/glutaminein antiport, pH 6.5, temperature not specified in the publication


organism: Bacillus anthracis

proof_lines: whole cell assay, pH not specified in the publication, temperature not specified in the publication


organism: Rattus norvegicus

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


organism: Serendipita indica

substrate_name: phosphate

proof_lines: pH and temperature not specified in the publication, iPT belongs to the high affinity phosphate transporter family

substrate: phosphate


organism: Escherichia coli


organism: Acidaminococcus fermentans


organism: Veillonella parvula

substrate_name: (S)-methylmalonyl-CoA

column_label: PDF text lines 468-469 state apparent K_m for (S)-methylmalonyl-CoA at 20 mM NaCl = 7 uM

raw_value_unit_evidence: apparent K_m = 7 uM

row_label: (S)-methylmalonyl-CoA apparent K_m

table_label: Results text / abstract kinetic summary

substrate: (S)-methylmalonyl-CoA


substrate_name: malonyl-CoA

column_label: PDF text reports that malonyl-CoA was also decarboxylated with apparent Km = 35 uM.

raw_value_unit_evidence: Km raw_value=35 raw_unit=uM

row_label: malonyl-CoA

table_label: Abstract/results prose kinetic summary for purified methylmalonyl-CoA decarboxylase

substrate: malonyl-CoA


column_label: PDF text lines 464-465 state apparent K_m for Na+ at 0.1 mM (S)-methylmalonyl-CoA of 0.6 mM

raw_value_unit_evidence: apparent K_m = 0.6 mM

row_label: Na+ apparent K_m


organism: Salmonella enterica subsp. enterica serovar Typhimurium


enzyme_display_name: arsenite-transporting ATPase

enzyme: arsenite-transporting ATPase


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP


enzyme_display_name: oxaloacetate decarboxylase (Na(+) extruding)

organism: Klebsiella aerogenes


substrate_name: Pyruvate

proof_lines: product inhibition competitive for oxaloacetate

enzyme: oxaloacetate decarboxylase (Na(+) extruding)

substrate: Pyruvate


organism: Synechococcus elongatus

substrate_name: nitrate

substrate: nitrate


substrate_name: nitrite

substrate: nitrite


substrate_name: ATP

sequence_variant_note: Mutation signature P172T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant P172T of the ATP-binding subunit HisP

substrate: ATP


sequence_variant_note: Mutation signature T205A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant T205A of the ATP-binding subunit HisP


substrate_name: arsenite

substrate: arsenite


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, in absence of SbIII
pH 7.5, in presence of SbIII


organism: Caenorhabditis elegans


organism: Propionigenium modestum


organism: Methanosarcina mazei

substrate_name: diphosphate

proof_lines: K0.5 value, Hill coefficient 4.27, presence of 50 mM NaCl, pH 7.2, 30°C

proof_lines: K0.5 value, Hill coefficient 3.74, pH 7.2, 30°C

proof_lines: K0.5 value, Hill coefficient 3.46, presence of 100 mM NaCl, pH 7.2, 30°C

substrate: diphosphate


proof_lines: pH 7.4, 37°C, wild-type enzyme in absence of Sb3+

proof_lines: pH 7.4, 37°C, wild-type enzyme in presence of Sb3+


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


substrate_name: oxaloacetate

substrate: oxaloacetate


organism: Homo sapiens

substrate_name: H2O; ATP; Mn2+

substrate: H2O; ATP; Mn2+


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Thermotoga maritima

substrate_name: Na+[side 1]

proof_lines:
40°C, pH 7.2
40°C, pH 7.2, presence of K+

substrate: Na+[side 1]


organism: Solanum tuberosum

substrate_name: phosphate/out

proof_lines: pH and temperature not specified in the publication

substrate: phosphate/out


proof_lines: yeast strain BY4762 lacking Sul1 and Sul2, transformed with SulT, 30°C, pH not specified in the publication


organism: Medicago truncatula

substrate_name: nitrate/out

proof_lines: recombinant enzyme in frog oocytes, pH 5.5, temperature not specified in the publication

substrate: nitrate/out


enzyme_display_name: ABC-type glutathione transporter

substrate_name: Unknown

enzyme: ABC-type glutathione transporter

substrate: Unknown


enzyme_display_name: bacterial ABC-type protein transporter

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
pH 8.0, 25°C, 200 mM NaCl
pH 8.0, 25°C, 100 mM NaCl
pH 8.0, 25°C, 50 mM NaCl

enzyme: bacterial ABC-type protein transporter


proof_lines: mutant K274I, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


proof_lines: mutant M154K, pH 7.5, temperature not specified in the publication


proof_lines: mutant L190V, pH 7.5, temperature not specified in the publication


proof_lines: mutant V252E, pH 7.5, temperature not specified in the publication


proof_lines: mutant F197I, pH 7.5, temperature not specified in the publication


proof_lines: mutant L324V, pH 7.5, temperature not specified in the publication


assay_conditions_summary: pH 7.4; 305.15 K; cofactor ATP


substrate_name: RRYQKSTEL

proof_lines: pH 6.0, 22°C, transfection of HeLa cells

proof_lines: pH 6.0, 22°C, transfection of Caco-2 cells

substrate: RRYQKSTEL


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 9; 303.15 K; cofactor ATP


enzyme_display_name: ABC-type oligopeptide transporter

organism: Metamycoplasma hominis

enzyme: ABC-type oligopeptide transporter


enzyme_display_name: ABC-type dipeptide transporter

organism: Hebeloma cylindrosporum

proof_lines: isoform Ptr2a, pH not specified in the publication, temperature not specified in the publication

proof_lines: isoform Ptr2b, pH not specified in the publication, temperature not specified in the publication

enzyme: ABC-type dipeptide transporter


proof_lines: pH 6.7, temperature not specified in the publication


organism: Equus asinus

proof_lines: pH 6.5, temperature not specified in the publication


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, full-length mtHsp70 in absence of Hep


enzyme_display_name: ABC-type maltose transporter

organism: Bacillus subtilis

substrate_name: maltose

proof_lines: Bacillus subtilis wild type, at 37°C, 0.001 mM 14C-labelled maltose (final concentration)

enzyme: ABC-type maltose transporter

substrate: maltose


proof_lines: Bacillus subtilis strain MD195, mutant enzyme amyE, at 37°C, 0.001 mM 14C-labelled maltose (final concentration)

proof_lines: Bacillus subtilis strain MD235, mutant enzyme mdxE, at 37°C, 0.001 mM 14C-labelled maltose (final concentration)


proof_lines:
mutant Q701H
mutant D668/Q701H


organism: Alicyclobacillus acidocaldarius


assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP


organism: Arabidopsis thaliana

proof_lines: nanodiscs formed by membrane scaffolding proteins and 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine, presence of 2.5 mM oxidized glutathione, pH 7.5, 25°C

proof_lines: nanodiscs formed by membrane scaffolding proteins and 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine, presence of 10 mM glutathione, pH 7.5, 25°C

proof_lines: nanodiscs formed by membrane scaffolding proteins and 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine, pH 7.5, 25°C


enzyme_display_name: protein-secreting ATPase

organism: Shigella flexneri

substrate_name: ATP; H2O

sequence_source: UniProtKB reviewed (Swiss-Prot) P0A1C1

enzyme: protein-secreting ATPase

substrate: ATP; H2O


organism: Salmonella enterica subsp. enterica serovar Typhimurium


enzyme_display_name: ABC-type oligosaccharide transporter

organism: Escherichia coli

proof_lines: KM-value with 50% of the enzyme being substrate-saturated, in the presence of 200 mM NaCl

proof_lines: KM-value with 50% of the enzyme being substrate-saturated, in the presence of 100 mM NaCl

proof_lines: KM-value with 50% of the enzyme being substrate-saturated, in the presence of 50 mM NaCl

enzyme: ABC-type oligosaccharide transporter


enzyme_display_name: ABC-type cystine transporter

substrate_name: L-cystine-[cystine-binding protein I][side 1]

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

proof_lines:
at pH and ?C
at pH 6.5 and 37°C

enzyme: ABC-type cystine transporter


substrate_name: ATP; RRYCKSTEL

substrate: ATP; RRYCKSTEL


substrate_name: a 9-mer oligopeptide

substrate: a 9-mer oligopeptide


organism: Thermococcus litoralis

substrate_name: ATP; Maltose; H2O

substrate: ATP; Maltose; H2O


enzyme_display_name: ABC-type methionine transporter

enzyme: ABC-type methionine transporter


sequence_variant_note: Mutation signature N229A/Y160A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme N229A/Y160A, at pH 6.5 and 37°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +30, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme N295A/N229A, at pH 6.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature N295A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature N229A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +4, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme N295A/M163A, at pH 6.5 and 37°C


enzyme_display_name: ABC-type antigen peptide transporter

enzyme: ABC-type antigen peptide transporter


organism: Rattus norvegicus


organism: Pseudomonas savastanoi pv. phaseolicola


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein-secreting ATPase(Enzyme) mutant delta 1-6


proof_lines: kcat is 0.22 sec(-1) for ATPase activity (monomeric form). kcat is 0.84 sec(-1) for ATPase activity (trimeric form). kcat is 0.41 sec(-1) for ATPase activity (monomeric form, in the presence of MxiN/SctL). kcat is 0.50 sec(-1) for ATPase ac


organism: Bos taurus

proof_lines: transfected Chinese hamster ovary cells, pH 6, 37°C


proof_lines: mutant carrying mutations in all 5 putative N-glycosylation sites, 37°C, pH not specified in the publication


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


organism: Homo sapiens


substrate_name: ATP (monomeric form)

substrate: ATP (monomeric form)


substrate_name: ATP


substrate_name: GTP

substrate: GTP


organism: Xanthomonas campestris

proof_lines: XpsE wild-type + MBP-tagged XpsL, residues 1-215

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature R286A to reconstruct the assayed variant sequence.

proof_lines: XpsE mutant R286A + MBP-tagged XpsL, residues 1-215


proof_lines: XpsE, N-domain removed + MBP-tagged XpsL, residues 1-215


organism: Legionella pneumophila

source_db: oed

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP

source: oed


organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)


substrate_name: CTP

substrate: CTP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: cofactor ATP


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; 298.15 K; cofactor ATP


column_label: PMC3983159 results prose states that the Km value for ATP was 0.81 +/- 0.02 mM.

raw_value_unit_evidence: Results prose reports SsaN ATP Km raw_value=0.81 raw_unit=mM.

row_label: Salmonella SPI-2 Type III secretion ATPase SsaN

table_label: PMC3983159 Figure 3D/3E results prose


assay_conditions_summary: pH 7; 305.15 K; cofactor ATP


organism: Aeromonas hydrophila

substrate_name: MgATP

proof_lines: pH 7.5, 37°C, ATPase activity of N-terminal cytoplasmic domain

substrate: MgATP


proof_lines: cosubstrate YCK(K8)STEL-[YCK(K8)STEL-binding protein][side 1], pH 7.5, 37°C

proof_lines: cosubstrate RRYQKSTELRRYQKSTEL-[RRYQKSTELRRYQKSTEL-binding protein][side 1], pH 7.5, 37°C

proof_lines: cosubstrate RRYQKSTEL-[RRYQKSTEL-binding protein][side 1], pH 7.5, 37°C


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

proof_lines: mutant N95CC treated with diamide, presence of DTT

proof_lines: mutant N95CC treated with diamide, absence of DTT


organism: Yersinia enterocolitica subsp. palearctica


proof_lines: subunit DotBL, at 25°C, pH not specified in the publication


organism: Pseudomonas syringae

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0, 30°C, monomeric form
pH 8.0, 30°C, dodecameric form


enzyme_display_name: ABC-type teichoic-acid transporter

organism: Bacillus subtilis

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: in the presence of 4.33 mM clodronate, at pH 7.5 and 22°C

proof_lines: in the presence of 2.16 mM clodronate, at pH 7.5 and 22°C

proof_lines: in the absence of clodronate, at pH 7.5 and 22°C

enzyme: ABC-type teichoic-acid transporter


organism: Salmonella enterica

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: purified recombinant SsaN-Myc-His6 enzyme, pH 8.0, 37°C


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines:
at pH 7.8 and 37°C
pH 7.8, 37°C


organism: Shigella flexneri

proof_lines:
pH 8, 22°C
at pH 7.9 and 25°C


organism: Escherichia coli


enzyme_display_name: P-type phospholipid transporter

proof_lines: pH 7.5, 37°C, KM value of purified, detergent-solubilized MsbA, whereas the KM value calculated in the presence of 0.05 mM KdO2-lipid A is decreased by more than half

enzyme: P-type phospholipid transporter


enzyme_display_name: ABC-type xenobiotic transporter

organism: Cyanidioschyzon merolae

substrate_name: nicardipine[side 1]

proof_lines: mutant enzyme W114Y/W161Y/W363Y/W364Y/M391W, at pH 7.5 and 37°C

enzyme: ABC-type xenobiotic transporter

substrate: nicardipine[side 1]


substrate_name: rhodamine 6G[side 1]

proof_lines: mutant enzyme W114Y/W161Y/W363Y/W364Y, at pH 7.5 and 37°C

substrate: rhodamine 6G[side 1]


organism: Candida albicans

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: in the presence of MalE, at pH 7.5 and 37°C

proof_lines: in the presence of MalE and maltose, at pH 7.5 and 37°C


organism: Poeciliopsis lucida

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


enzyme_display_name: ABC-type fatty-acyl-CoA transporter

enzyme: ABC-type fatty-acyl-CoA transporter


organism: Saccharomyces cerevisiae

substrate_name: UTP

substrate: UTP


proof_lines: enzyme in plasma membrane, at pH 9.5 and 30°C


proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


proof_lines:
pH 7.5, 37°C
at pH 9.5 and 30°C


organism: Mus musculus

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)thioxanthylium hexafluorophosphate

proof_lines: pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)selenoxanthylium hexafluorophosphate

proof_lines: pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-methoxyphenyl)-xanthylium hexafluorophosphate


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature Q1118A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q1118A, in the absence of nicardipine, at 37°C, pH not specified in the publication

proof_lines: mutant enzyme Q1118A, in the presence of 0.05 mM nicardipine, at 37°C, pH not specified in the publication


proof_lines: GST-fused form of nucleotide-binding domain 1 of the enzyme MRP1, at pH 7.5 and 30°C

proof_lines: GST-fused form of nucleotide-binding domain 2 of the enzyme MRP1, at pH 7.5 and 30°C


substrate_name: Dioleoyl phosphatidylserine; ATP; H2O

substrate: Dioleoyl phosphatidylserine; ATP; H2O


substrate_name: H2O; ATP; Dioleoyl phosphatidylserine

substrate: H2O; ATP; Dioleoyl phosphatidylserine


organism: Leucoraja erinaceus

assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP

proof_lines: with S-(2,4-dinitrophenyl)glutathione as cosubstrate, at pH 7.5 and 20°C

proof_lines: with S-glutathione as cosubstrate, at pH 7.5 and 20°C


substrate_name: 17-beta-estradiol 17-(beta-D-glucuronide) (at 37 degrees Celsius)


substrate_name: DHEAS transport

substrate: DHEAS transport


substrate_name: ATP; H2O


organism: Streptomyces peucetius

substrate_name: doxorubicin/in

proof_lines: in the presence of ATP, at pH 7.5 and 37°C

substrate: doxorubicin/in


substrate: 17-beta-estradiol 17-(beta-D-glucuronide) (at 37 degrees Celsius)


enzyme_display_name: ABC-type heme transporter

substrate_name: Hemin; H2O; ATP

enzyme: ABC-type heme transporter

substrate: Hemin; H2O; ATP


substrate_name: Unknown

substrate: Unknown


organism: Plasmodium falciparum (isolate 3D7)


organism: Rattus norvegicus


organism: Bos taurus


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


substrate_name: 17beta-glucuronosyl [6,7-3H]oestradiol

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature R1297H to reconstruct the assayed variant sequence.

proof_lines: vesicles from MRP3-Arg1297His transfected cells

substrate: 17beta-glucuronosyl [6,7-3H]oestradiol


substrate_name: estradiol 17-beta-D-glucuronide/in

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature W995Y with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: estradiol 17-beta-D-glucuronide/in


substrate_name: leukotriene C4/in

proof_lines:
at pH 7.5 and 37°C
pH 7.4, 37°C, recombinant BCRP
pH 7.4, 37°C

substrate: leukotriene C4/in


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: arsenic triglutathione[side 1]

proof_lines: pH and temperature not specified in the publication

substrate: arsenic triglutathione[side 1]


substrate_name: monomethylarsonous acid diglutathione[side 1]

sequence_variant_note: Mutation signature Y920F/S921A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y920F/S921A, expressed in HEK-293 cells, at 37°C, pH not specified in the publication


substrate_name: S-(leukotriene C4)glutathione[side 1]

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

proof_lines: wild type enzyme, at 23°C, pH not specified in the publication

proof_lines: wild type enzyme, expressed in HEK-293 cells, at 37°C, pH not specified in the publication

proof_lines: wild type enzyme, expressed in HeLa cells, at 37°C, pH not specified in the publication

substrate: S-(leukotriene C4)glutathione[side 1]


proof_lines: mutant enzyme, at 23°C, pH not specified in the publication


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K380R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: xenobiotic-transporting ATPase(Enzyme) mutant K380R

substrate: ATP; H2O


substrate_name: H2O; ATP

substrate: H2O; ATP


proof_lines:
vesicles from MRP3 cells
pH 7, 37°C, MRP3


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V906A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant V906A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant V906A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E371Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E371Q, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L367A to reconstruct the assayed variant sequence.

proof_lines: mutant L367A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant L367A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
phosphatase activity
phosphatidylserine translocase activity
pH 7.5, 37°C


substrate_name: acetyl phosphate

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

proof_lines:
phosphatase activity
phosphatidylserine translocase activity

substrate: acetyl phosphate


substrate_name: p-nitrophenyl phosphate

proof_lines: phosphatase activity, detection of p-nitrophenolate formation from trichloroacetic acid precipitates

proof_lines: phosphatase activity, continous detection of p-nitrophenolate formation in ghost at neutral pH

substrate: p-nitrophenyl phosphate


substrate_name: cholylglycine (in the presence of 5 mM GSH)

column_label: Table 2 | row Cholylglycine | column Km, uM | raw 25.8+/-0.8 uM | normalized central value 0.0258 mM | condition bile acid + 5 mM GSH.

normalized_value_unit_evidence: 25.8+/-0.8 uM = 0.0258+/-0.0008 mM; exported Km 0.0258 mM matches the normalized central value.

raw_value_unit_evidence: Table 2 row Cholylglycine; column Km, uM; raw value 25.8+/-0.8 uM.

row_label: cholylglycine

table_label: Table 2. Kinetic constants for ABCC4-mediated bile acid cotransport in the presence of 5 mM GSH


substrate_name: cholyltaurine (in the presence of 5 mM GSH)

column_label: Table 2 | row Cholyltaurine | column Km, uM | raw 7.7+/-0.3 uM | normalized central value 0.0077 mM | condition bile acid + 5 mM GSH.

normalized_value_unit_evidence: 7.7+/-0.3 uM = 0.0077+/-0.0003 mM; exported Km 0.0077 mM matches the normalized central value.

raw_value_unit_evidence: Table 2 row Cholyltaurine; column Km, uM; raw value 7.7+/-0.3 uM.

row_label: cholyltaurine


substrate_name: deoxycholylglycine (in the presence of 5 mM GSH)


substrate_name: chenodeoxycholylglycine (in the presence of 5 mM GSH)

column_label: Table 2 | row Chenodeoxycholylglycine | column Km, uM | raw 5.9+/-0.3 uM | normalized central value 0.0059 mM | condition bile acid + 5 mM GSH.

normalized_value_unit_evidence: 5.9+/-0.3 uM = 0.0059+/-0.0003 mM; exported Km 0.005900000000000001 mM matches the normalized central value.

raw_value_unit_evidence: Table 2 row Chenodeoxycholylglycine; column Km, uM; raw value 5.9+/-0.3 uM.

row_label: chenodeoxycholylglycine


substrate_name: chenodeoxycholyltaurine (in the presence of 5 mM GSH)

column_label: Table 2 | row Chenodeoxycholyltaurine | column Km, uM | raw 3.6+/-0.1 uM | normalized central value 0.0036 mM | condition bile acid + 5 mM GSH.

normalized_value_unit_evidence: 3.6+/-0.1 uM = 0.0036+/-0.0001 mM; exported Km 0.0036000000000000003 mM matches the normalized central value.

raw_value_unit_evidence: Table 2 row Chenodeoxycholyltaurine; column Km, uM; raw value 3.6+/-0.1 uM.

row_label: chenodeoxycholyltaurine


substrate_name: cholate (in the presence of 5 mM GSH)

column_label: Table 2 | row Cholate | column Km, uM | raw 14.8+/-0.8 uM | normalized central value 0.0148 mM | condition bile acid + 5 mM GSH.

normalized_value_unit_evidence: 14.8+/-0.8 uM = 0.0148+/-0.0008 mM; exported Km 0.0148 mM matches the normalized central value.

raw_value_unit_evidence: Table 2 row Cholate; column Km, uM; raw value 14.8+/-0.8 uM.

row_label: cholate

substrate: cholate (in the presence of 5 mM GSH)


substrate_name: glutathione (in the presence of 10 uM of hemin)


substrate_name: hemin (in the presence of 1 mM of glutathione)

column_label: Figure 4 caption, panel b, reports K_M for hemin in addition of GSH 1 mM as 190 +/- 23 nM.

raw_value_unit_evidence: Km raw_value=190 +/- 23 raw_unit=nM.

row_label: hemin / GSH 1 mM

table_label: PMID 33007128 Figure 4


substrate_name: hematin (in the presence of 1 mM of glutathione)

column_label: Figure 4 caption, panel c, reports K_M for hematin in addition of GSH 1 mM as 600 +/- 140 nM.

raw_value_unit_evidence: Km raw_value=600 +/- 140 raw_unit=nM.

row_label: hematin / GSH 1 mM


substrate_name: Fe-coproporphyrin III (in the presence of 1 mM of glutathione)

column_label: Figure 4 caption, panel d, reports K_M for Fe-coproporphyrin III in addition of GSH 1 mM as 148 +/- 41 nM.

raw_value_unit_evidence: Km raw_value=148 +/- 41 raw_unit=nM.

row_label: Fe-coproporphyrin III / GSH 1 mM


substrate_name: lumefantrine

substrate: lumefantrine


substrate_name: mefloquine

substrate: mefloquine


substrate_name: chloroquine

substrate: chloroquine


substrate_name: quinine

substrate: quinine


enzyme_display_name: ABC-type polyamine transporter

proof_lines:
at pH 7.4 and 37°C
at pH 9.6 and 37°C

enzyme: ABC-type polyamine transporter


enzyme_display_name: ABC-type quaternary amine transporter

substrate_name: ATP

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: 22°C, pH 8.0, 0.15 M NaCl, monomeric and dimeric OpuAA

enzyme: ABC-type quaternary amine transporter


substrate_name: estrone 3-sulfate

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

substrate: estrone 3-sulfate


substrate_name: 4-methylumbelliferone sulfate

column_label: The abstract reports 4-methylumbelliferone sulfate was transported by ABCG2 with Km = 12.9 microm.

raw_value_unit_evidence: Km raw_value=12.9 microm raw_unit=microM

row_label: Prose segment: 4-methylumbelliferone sulfate Km

table_label: PubMed PMID 12682043 abstract

substrate: 4-methylumbelliferone sulfate


proof_lines: pH 8.0, 37°C, wild-type, presence of valinomycin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature Y1040W to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, mutant Y1040W, presence of verapamil

proof_lines: pH 8.0, 37°C, mutant Y1040W, presence of valinomycin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature Y397W to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, mutant Y397W, presence of verapamil

proof_lines: pH 8.0, 37°C, mutant Y397W, presence of valinomycin

proof_lines: pH 8.0, 37°C, mutant Y397W, presence of FK506


enzyme_display_name: ABC-type putrescine transporter

substrate_name: putrescine-[putrescine-binding protein PotF][side 1]

proof_lines: pH and temperature not specified in the publication

enzyme: ABC-type putrescine transporter


enzyme_display_name: ABC-type vitamin B12 transporter

substrate_name: Unknown

enzyme: ABC-type vitamin B12 transporter

substrate: Unknown


substrate_name: cholylglycine (in the presence of 5 mM GSH)


substrate_name: cholyltaurine (in the presence of 5 mM GSH)


substrate_name: deoxycholylglycine (in the presence of 5 mM GSH)


substrate_name: chenodeoxycholylglycine (in the presence of 5 mM GSH)


substrate_name: chenodeoxycholyltaurine (in the presence of 5 mM GSH)


substrate_name: cholate (in the presence of 5 mM GSH)


substrate_name: ATP; H2O


substrate_name: Dioleoyl phosphatidylserine; H2O; ATP

substrate: Dioleoyl phosphatidylserine; H2O; ATP


substrate_name: phosphatidylethanolamine and for ATPase activity (at 37 degrees Celsius and at pH 7.4)


organism: Arabidopsis thaliana

substrate_name: E(2)17betaG (at pH 8.0 and 25 degrees Celsius)


substrate_name: DNP-GS (at pH 8)

substrate: DNP-GS (at pH 8)


substrate_name: DNB-GS (at pH 7.4 and 25 degrees Celsius)


substrate_name: ATP (determined by measuring estradiol-17-beta-o-glucuronide transport)

verification_status: corrected

column_label: JBC Results paragraph states apparent Km values for ATP were 1.36 and 0.66 mM by measuring initial rates of ATP-dependent uptake of [3H]E217betaG and [3H]TC, respectively; Figure 5 caption defines the E217betaG and TC assay panels.

normalized_value_unit_evidence: Paper normalized_value=1.36 normalized_unit=mM; queued row normalized_value=0.00136 mM.

raw_value_unit_evidence: Paper reports apparent Km for ATP raw_value=1.36 raw_unit=mM for [3H]E217betaG uptake.

row_label: ATP concentration dependence measured by [3H]E217betaG uptake

table_label: Results paragraph and Figure 5

status: corrected


substrate_name: taurolithocholate sulfate

column_label: PubMed abstract reports K(m) and V(max) values for uptake of TC and TLC-S; for TLC-S, K(m)=3.06 +/- 0.57 microM.

normalized_value_unit_evidence: Km normalized_value=0.00306 normalized_unit=mM converted from 3.06 microM.

raw_value_unit_evidence: Km raw_value=3.06 +/- 0.57 raw_unit=microM for uptake of TLC-S; abstract also reports Vmax=161.9 +/- 21.7 pmol/min/mg of protein.

table_label: PubMed abstract kinetic prose

substrate: taurolithocholate sulfate


substrate_name: taurocholate

column_label: PubMed abstract reports K(m) and V(max) values for uptake of TC and TLC-S; for TC, K(m)=15.9 +/- 4.9 microM.

normalized_value_unit_evidence: Km normalized_value=0.0159 normalized_unit=mM converted from 15.9 microM.

raw_value_unit_evidence: Km raw_value=15.9 +/- 4.9 raw_unit=microM for uptake of TC; abstract also reports Vmax=50.1 +/- 9.3 pmol/min/mg of protein.

row_label: taurocholate (TC) uptake

substrate: taurocholate


column_label: PubMed abstract reports apparent K(m) values for ATP were 1.36 and 0.66 mM at 55 nM [3H]E2-17betaG and 1.2 microM [3H]TC, respectively; current row is the E2-17betaG condition.

raw_value_unit_evidence: Apparent Km raw_value=1.36 raw_unit=mM for ATP when uptake of [3H]E2-17betaG was measured at 55 nM.

row_label: ATP concentration dependence measured by [3H]E2-17betaG uptake

substrate: ATP (determined by measuring estradiol-17-beta-o-glucuronide transport)


substrate_name: GSSG (at pH 8)

substrate: GSSG (at pH 8)


substrate_name: Bn-NCC-1 (at pH 8)

substrate: Bn-NCC-1 (at pH 8)


substrate_name: prostaglandin E1

column_label: Fig. 2: Time and concentration dependence of PGE1 and PGE2 transport by MRP4; Results prose reporting apparent Km and Vmax values; Fig. 2B; results prose reports apparent Km 2.1 uM for prostaglandin E1.

normalized_value_unit_evidence: Km=0.0021 mM for prostaglandin E1 after uM -> mM conversion.

raw_value_unit_evidence: Results prose adjacent to Fig. 2 reports apparent Km 2.1 uM for prostaglandin E1.

row_label: PGE1 / prostaglandin E1, Fig. 2B

substrate: prostaglandin E1


substrate_name: prostaglandin E2

column_label: Fig. 2: Time and concentration dependence of PGE1 and PGE2 transport by MRP4; Results prose reporting apparent Km and Vmax values; Fig. 2D; results prose reports apparent Km 3.4 uM for prostaglandin E2.

normalized_value_unit_evidence: Km=0.0034 mM for prostaglandin E2 after uM -> mM conversion.

raw_value_unit_evidence: Results prose adjacent to Fig. 2 reports apparent Km 3.4 uM for prostaglandin E2.

row_label: PGE2 / prostaglandin E2, Fig. 2D

substrate: prostaglandin E2


substrate_name: ATP (in the presence of PS)

substrate: ATP (in the presence of PS)


organism: Aphanothece halophytica

substrate_name: betaine

proof_lines: Aphanothece halophytica cells supplemented with 0.5 M NaCl

proof_lines: Aphanothece halophytica cells supplemented with 2.0 M NaCl

proof_lines: at pH 8.5, Aphanothece halophytica cells

substrate: betaine


substrate_name: H2O; ATP

substrate: H2O; ATP


substrate_name: leukotriene C4

substrate: leukotriene C4


substrate_name: bilirubin-glucuronoside

column_label: Article abstract kinetic prose / human MRP2 / MGB: Km 0.7 micromol/L; normalized Km 0.0007 mM.

raw_value_unit_evidence: K(m) values were 0.7 and 0.9 micromol/L for human MRP2, and 0.8 and 0.5 micromol/L for rat MRP2, with MGB and BGB as substrates, respectively. Matched row: human MRP2 / MGB; raw Km 0.7 micromol/L.

row_label: human MRP2 / MGB

table_label: Article abstract / recombinant human and rat MRP2 Km values for bilirubin conjugates

substrate: bilirubin-glucuronoside


substrate_name: bilirubin-bisglucuronoside

column_label: Article abstract kinetic prose / human MRP2 / BGB: Km 0.9 micromol/L; normalized Km 0.0009 mM.

raw_value_unit_evidence: K(m) values were 0.7 and 0.9 micromol/L for human MRP2, and 0.8 and 0.5 micromol/L for rat MRP2, with MGB and BGB as substrates, respectively. Matched row: human MRP2 / BGB; raw Km 0.9 micromol/L.

row_label: human MRP2 / BGB

substrate: bilirubin-bisglucuronoside


substrate_name: cAMP

column_label: The abstract reports MRP5-mediated transport of 3',5'-cyclic AMP with a Km value of 379 micrometer.

raw_value_unit_evidence: Km raw_value=379 micrometer raw_unit=microM

row_label: Prose segment: cAMP Km

table_label: PubMed PMID 10893247 abstract

substrate: cAMP


substrate_name: cGMP

column_label: The abstract reports ATP-dependent transport of 3',5'-cyclic GMP was saturable with a Km value of 2.1 micrometer.

raw_value_unit_evidence: Km raw_value=2.1 micrometer raw_unit=microM

row_label: Prose segment: cGMP Km

substrate: cGMP


substrate_name: urate

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

column_label: Abstract and Table 1, row [14C]urate, Km column = 1,550 +/- 270 uM; abstract reports 1.5 +/- 0.3 mM

normalized_value_unit_evidence: 1.5 mM (table normalized 1.55 mM)

table_label: Table 1

substrate: urate


column_label: Abstract and Table 1, row [3H]cGMP, Km column = 180 +/- 20 uM; abstract reports 180 +/- 20 uM

normalized_value_unit_evidence: 0.18 mM (table normalized 0.18 mM)


column_label: The abstract reports LTC4 transport by ABCC4 with a Km of 0.13 microM in vesicles from fibroblasts.

raw_value_unit_evidence: Km raw_value=0.13 microM raw_unit=microM

row_label: Prose segment: LTC4 Km

table_label: PubMed PMID 17959747 abstract


substrate_name: LTB4 (in the presence of 5 mM GSH)

smiles: CCCCCC=CCC(C=CC=CC=CC(CCCC(=O)O)O)O

column_label: The abstract reports LTB4 Km values of 5.2 microM with vesicles from fibroblasts and notes transport occurs in the presence of reduced glutathione.

raw_value_unit_evidence: Km raw_value=5.2 microM raw_unit=microM

row_label: Prose segment: LTB4 Km with GSH

substrate: LTB4 (in the presence of 5 mM GSH)


substrate_name: folate

column_label: The abstract reports MRP5 transports folic acid with KM = 1.0 mmol/L.

raw_value_unit_evidence: KM raw_value=1.0 mmol/L raw_unit=mmol/L

row_label: Prose segment: folic acid KM

table_label: PubMed PMID 15899835 abstract

substrate: folate


substrate_name: methotrexate

column_label: The abstract reports MRP5 transports MTX with KM = 1.3 mmol/L.

raw_value_unit_evidence: KM raw_value=1.3 mmol/L raw_unit=mmol/L

row_label: Prose segment: MTX KM

substrate: methotrexate


column_label: Article abstract kinetic prose / rat MRP2 / MGB: Km 0.8 micromol/L; normalized Km 0.0008 mM.

raw_value_unit_evidence: K(m) values were 0.7 and 0.9 micromol/L for human MRP2, and 0.8 and 0.5 micromol/L for rat MRP2, with MGB and BGB as substrates, respectively. Matched row: rat MRP2 / MGB; raw Km 0.8 micromol/L.

row_label: rat MRP2 / MGB


column_label: Article abstract kinetic prose / rat MRP2 / BGB: Km 0.5 micromol/L; normalized Km 0.0005 mM.

raw_value_unit_evidence: K(m) values were 0.7 and 0.9 micromol/L for human MRP2, and 0.8 and 0.5 micromol/L for rat MRP2, with MGB and BGB as substrates, respectively. Matched row: rat MRP2 / BGB; raw Km 0.5 micromol/L.

row_label: rat MRP2 / BGB


column_label: Primary article prose states the LTC4 Km directly in the MRP transport paragraph.

raw_value_unit_evidence: LTC4 had the highest affinity for this transporter with a Km of 97 nM

row_label: MRP-transfected HeLa cell membrane vesicles; 190-kDa MRP transporter

table_label: Article text paragraph (ScienceDirect/JBC article; no table)


substrate_name: ATP

column_label: Primary article prose states the ATP Km directly in the MRP transport paragraph.

normalized_value_unit_evidence: 19 microM = 0.019 mM

raw_value_unit_evidence: Km for ATP was 19 microM

substrate: ATP


substrate_name: ZJ43 (glutamate analog)

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

column_label: Exact metric-labeled prose/figure evidence: concentration-dependent transport fits Michaelis-Menten kinetics with Km for ZJ43 (1.9 mM), linked to Figure 8D concentration-dependent ZJ43 transport.

normalized_value_unit_evidence: Km normalized_value=1.9 normalized_unit=mM from raw 1.9 mM.

raw_value_unit_evidence: Main text reports Km for ZJ43 = 1.9 mM; Figure 8 caption identifies panel D as various concentrations of ZJ43 fitted to Michaelis-Menten kinetics.

row_label: ZJ43 Figure 8D concentration-dependent transport curve

table_label: PMC4683265 main text and Figure 8

substrate: ZJ43 (glutamate analog)


substrate_name: N-acetylaspartylglutamate (NAAG)

column_label: Exact metric-labeled prose/figure evidence: concentration-dependent transport fits Michaelis-Menten kinetics with Km for NAAG (3.5 mM), linked to Figure 8C concentration-dependent NAAG transport.

normalized_value_unit_evidence: Km normalized_value=3.5 normalized_unit=mM from raw 3.5 mM.

raw_value_unit_evidence: Main text reports Km for NAAG = 3.5 mM; Figure 8 caption identifies panel C as various concentrations of NAAG fitted to Michaelis-Menten kinetics.

row_label: NAAG Figure 8C concentration-dependent transport curve

substrate: N-acetylaspartylglutamate (NAAG)


substrate_name: N-ethylmaleimide S-glutathione

substrate: N-ethylmaleimide S-glutathione


enzyme_display_name: UniProt P31327

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P31327

source: skid


substrate_name: N-acetylglutamate

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

substrate: N-acetylglutamate


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.4


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.6


substrate_name: prostaglandin E1

column_label: Fig. 2: Time and concentration dependence of PGE1 and PGE2 transport by MRP4; Results prose reporting apparent Km and Vmax values; Fig. 2B; results prose reports apparent Km 2.1 uM for prostaglandin E1.

substrate: prostaglandin E1


substrate_name: prostaglandin E2

column_label: Fig. 2: Time and concentration dependence of PGE1 and PGE2 transport by MRP4; Results prose reporting apparent Km and Vmax values; Fig. 2D; results prose reports apparent Km 3.4 uM for prostaglandin E2.

substrate: prostaglandin E2


organism: Oryctolagus cuniculus

substrate_name: biotin

substrate: biotin


enzyme_display_name: biotin--[biotin carboxyl-carrier protein] ligase

organism: Botrytis cinerea

proof_lines: substrate from Caenorhabditis albicans, pH 8, 37°C

proof_lines: substrate from Staphylococcus aureus, pH 8, 37°C

proof_lines: substrate from Saccharomyces cerevisiae, pH 8, 37°C


enzyme: biotin--[biotin carboxyl-carrier protein] ligase


enzyme_display_name: ABC-type lipopolysaccharide transporter

organism: Escherichia coli

enzyme: ABC-type lipopolysaccharide transporter


proof_lines: mutant enzyme R144H/F239A, at pH 8.0 and 30°C


enzyme_display_name: glutamate--methylamine ligase

organism: Rhodovulum sp. 12E13

substrate_name: ethylamine

smiles: CCN

enzyme: glutamate--methylamine ligase

substrate: ethylamine


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


substrate_name: methylamine

smiles: CN

substrate: methylamine


substrate_name: Propylamine

smiles: CCCN

substrate: Propylamine


substrate_name: ammonium chloride

substrate: ammonium chloride


enzyme_display_name: carbamoyl-phosphate synthase (ammonia)

organism: Lithobates sylvaticus

proof_lines: freeze-exposed protein, presence of 100 mM urea, pH 7.4, 22°C

proof_lines: freeze-exposed protein, presence of 400 mM glucose, pH 7.4, 22°C

enzyme: carbamoyl-phosphate synthase (ammonia)


assay_conditions_summary: pH 7.4; 295.15 K; cofactor ATP

proof_lines: presence of 400 mM glucose, pH 7.4, 22°C


substrate_name: hydrogencarbonate

substrate: hydrogencarbonate


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: 1.3 S subunit of apotranscarboxylase

substrate: 1.3 S subunit of apotranscarboxylase


substrate_name: leukotriene C4

substrate: leukotriene C4


organism: Pyrococcus abyssi

proof_lines: pH 8.0, deletion mutant lacking the last 13 residues of the carboxyl end


proof_lines:
NaHCO3, 37°C, pH 8
NaHCO3, 70°C, pH 7.5


proof_lines: pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver


organism: Gallus gallus

assay_conditions_summary: cofactor CoA


enzyme_display_name: ABC-type L-arabinose transporter

organism: Trichoderma reesei

enzyme: ABC-type L-arabinose transporter


enzyme_display_name: ABC-type lipid A-core oligosaccharide transporter

organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: recombinant His-tagged wild-type enzyme, ATPase activity, pH 7.5, 37°C


proof_lines: enzyme in facial amphiphile FA-3 at pH 7.5 and 37°C

enzyme: ABC-type lipid A-core oligosaccharide transporter


organism: Penicillium chrysogenum

proof_lines: pH and temperature not specified in the publication


substrate_name: (+)-biotin

substrate: (+)-biotin


organism: Homo sapiens

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A1378T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A1378T, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C

substrate: ATP


organism: Bos taurus