IED Industry Enzyme Database

Detail Information for IndEnz0010001197
IED ID IndEnz0010001197
Enzyme Type ID esterase001197
Protein Name Carbonic anhydrase 1
EC 4.2.1.1
Carbonate dehydratase I
Carbonic anhydrase B
CAB
Carbonic anhydrase I
CA-I
Cyanamide hydratase CA1
EC 4.2.1.69
Gene Name CA1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF
Enzyme Length 261
Uniprot Accession Number P00915
Absorption
Active Site ACT_SITE 65; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00918
Activity Regulation ACTIVITY REGULATION: Activated by histamine, imidazole, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, sulfonamide derivatives such as acetazolamide, benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide), and 'prong inhibitors' BR15, BR17, BR22 and BR30. Activated by a short exposition to Foscarnet (phosphonoformate trisodium salt), but inhibited by a long one. Esterase activity weakly reduced by cyanamide. {ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}.
Binding Site BINDING 200; /note=Substrate; /evidence=ECO:0000269|PubMed:8057362
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:18618712}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000269|PubMed:10550681};
DNA Binding
EC Number 4.2.1.1; 4.2.1.69
Enzyme Function FUNCTION: Catalyzes the reversible hydration of carbon dioxide (PubMed:10550681, PubMed:18618712). Can hydrate cyanamide to urea (PubMed:10550681). {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:18618712}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (16); Binding site (1); Chain (1); Domain (1); Helix (9); Initiator methionine (1); Metal binding (6); Modified residue (1); Natural variant (3); Region (3); Sequence conflict (2); Turn (4)
Keywords 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Lyase;Metal-binding;Reference proteome;Zinc
Interact With Q12800
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196"
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (41)
Cross Reference PDB 1AZM; 1BZM; 1CRM; 1CZM; 1HCB; 1HUG; 1HUH; 1J9W; 1JV0; 2CAB; 2FOY; 2FW4; 2IT4; 2NMX; 2NN1; 2NN7; 3LXE; 3W6H; 3W6I; 4WR7; 4WUP; 4WUQ; 5E2M; 5GMM; 6EVR; 6EX1; 6F3B; 6FAF; 6FAG; 6G3V; 6HWZ; 6I0J; 6I0L; 6SWM; 6XZE; 6XZO; 6XZS; 6XZX; 6XZY; 6Y00; 7Q0D;
Mapped Pubmed ID 120192; 13911449; 14675565; 1554744; 15836783; 15837325; 16038020; 17427958; 17464559; 17968930; 19536309; 20349499; 20493921; 20505865; 20578724; 20624682; 21143847; 21282642; 2169869; 21900206; 21988832; 22001224; 22360420; 22416960; 22619369; 22838845; 22996014; 234739; 23557951; 24670789; 25165709; 25416956; 26079542; 26232327; 26459317; 26475450; 27413740; 27475498; 28001003; 28270370; 28445001; 28544359; 28613396; 28782909; 29635168; 29962205; 30344913; 30560259; 3080418; 30916466; 31419777; 31963697; 32031891; 32272689; 32992797; 33682938; 35008553; 4994926; 6407977; 6433979; 6819139; 8083199; 8399223; 9336012; 9635771;
Motif
Gene Encoded By
Mass 28,870
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.0 mM for CO(2) {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:18618712}; KM=15 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:18618712};
Metal Binding METAL 65; /note="Zinc 2; in variant Michigan-1"; /evidence="ECO:0000269|PubMed:12009884"; METAL 68; /note="Zinc 2; in variant Michigan-1"; /evidence="ECO:0000269|PubMed:12009884"; METAL 95; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362"; METAL 97; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362"; METAL 120; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362"; METAL 201; /note="Zinc 2; in variant Michigan-1"; /evidence="ECO:0000269|PubMed:12009884"
Rhea ID RHEA:10748; RHEA:23056
Cross Reference Brenda 4.2.1.1;