ID   CYNT_ECO57              Reviewed;         219 AA.
AC   P0ABF0; P17582; P78278;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=Carbonic anhydrase 1 {ECO:0000250|UniProtKB:P0ABE9};
DE            EC=4.2.1.1 {ECO:0000250|UniProtKB:P0ABE9};
DE   AltName: Full=Carbonate dehydratase 1 {ECO:0000250|UniProtKB:P0ABE9};
GN   Name=cynT; OrderedLocusNames=Z0435, ECs0392;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Carbon dioxide formed
CC       in the bicarbonate-dependent decomposition of cyanate by cyanase (CynS)
CC       diffuses out of the cell faster than it would be hydrated to
CC       bicarbonate, so the apparent function of this enzyme is to catalyze the
CC       hydration of carbon dioxide and thus prevent depletion of cellular
CC       bicarbonate. {ECO:0000250|UniProtKB:P0ABE9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate + H(+) = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P0ABE9};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0ABE9};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0ABE9};
CC   -!- SUBUNIT: Oligomer. {ECO:0000250|UniProtKB:P0ABE9}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005174; AAG54688.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33815.2; -; Genomic_DNA.
DR   PIR; D85528; D85528.
DR   PIR; H90677; H90677.
DR   RefSeq; NP_308419.2; NC_002695.2.
DR   RefSeq; WP_000658652.1; NZ_AP018488.1.
DR   AlphaFoldDB; P0ABF0; -.
DR   SMR; P0ABF0; -.
DR   STRING; 155864.Z0435; -.
DR   GeneID; 75202502; -.
DR   GeneID; 914494; -.
DR   KEGG; ece:Z0435; -.
DR   KEGG; ecs:ECs_0392; -.
DR   PATRIC; fig|386585.9.peg.487; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_053879_5_3_6; -.
DR   OMA; MPNVAAW; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0004089; F:carbonate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   CDD; cd00884; beta_CA_cladeB; 1.
DR   FunFam; 3.40.1050.10:FF:000004; Carbonic anhydrase; 1.
DR   Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR   InterPro; IPR045066; Beta_CA_cladeB.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR015892; Carbonic_anhydrase_CS.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11002:SF42; CARBONIC ANHYDRASE 1; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR   PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..219
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000077460"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
SQ   SEQUENCE   219 AA;  23764 MW;  5EB41F125EC4D731 CRC64;
     MKEIIDGFLK FQREAFPKRE ALFKQLATQQ SPRTLFISCS DSRLVPELVT QREPGDLFVI
     RNAGNIVPSY GPEPGGVSAS VEYAVAALRV SDIVICGHSN CGAMTAIASC QCMDHMPAVS
     HWLRYADSAR VVNEARPHSD LPSKAAAMVR ENVIAQLANL QTHPSVRLAL EEGRIALHGW
     VYDIESGSIA AFDGATRQFV PLAANPRVCA IPLRQPTAA
//