(data stored in ACNUC7421 zone)

SWISSPROT: CYNT_ECO57

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   05-JUL-2017, entry version 72.
DE   RecName: Full=Carbonic anhydrase 1;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase 1;
GN   Name=cynT; OrderedLocusNames=Z0435, ECs0392;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Carbon dioxide
CC       formed in the bicarbonate-dependent decomposition of cyanate by
CC       cyanase (CynS) diffuses out of the cell faster than it would be
CC       hydrated to bicarbonate, so the apparent function of this enzyme
CC       is to catalyze the hydration of carbon dioxide and thus prevent
CC       depletion of cellular bicarbonate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Oligomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG54688.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33815.1; -; Genomic_DNA.
DR   PIR; D85528; D85528.
DR   PIR; H90677; H90677.
DR   RefSeq; NP_308419.1; NC_002695.1.
DR   RefSeq; WP_000658652.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; P0ABF0; -.
DR   SMR; P0ABF0; -.
DR   STRING; 155864.Z0435; -.
DR   EnsemblBacteria; AAG54688; AAG54688; Z0435.
DR   EnsemblBacteria; BAB33815; BAB33815; BAB33815.
DR   GeneID; 914494; -.
DR   KEGG; ece:Z0435; -.
DR   KEGG; ecs:ECs0392; -.
DR   PATRIC; fig|386585.9.peg.487; -.
DR   eggNOG; ENOG4107B2H; Bacteria.
DR   eggNOG; COG0288; LUCA.
DR   HOGENOM; HOG000125182; -.
DR   KO; K01673; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   Gene3D; 3.40.1050.10; -; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR015892; Carbonic_anhydrase_CS.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; SSF53056; 1.
DR   PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0ABF0.
DR   SWISS-2DPAGE; P0ABF0.
KW   Complete proteome; Lyase; Metal-binding; Zinc.
FT   CHAIN         1    219       Carbonic anhydrase 1.
FT                                /FTId=PRO_0000077460.
FT   METAL        39     39       Zinc. {ECO:0000250}.
FT   METAL        41     41       Zinc. {ECO:0000250}.
FT   METAL        98     98       Zinc. {ECO:0000250}.
FT   METAL       101    101       Zinc. {ECO:0000250}.
FT   CONFLICT     59     59       V -> G (in Ref. 2; BAB33815).
FT                                {ECO:0000305}.
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
//

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