(data stored in ACNUC10821 zone)

SWISSPROT: C8U1J6_ECO10

ID   C8U1J6_ECO10            Unreviewed;       220 AA.
AC   C8U1J6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   Name=can {ECO:0000313|EMBL:BAI29004.1};
GN   OrderedLocusNames=ECO103_0126 {ECO:0000313|EMBL:BAI29004.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29004.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29004.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O;
CC         Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU003956};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|RuleBase:RU003956}.
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DR   EMBL; AP010958; BAI29004.1; -; Genomic_DNA.
DR   RefSeq; WP_000651599.1; NC_013353.1.
DR   SMR; C8U1J6; -.
DR   EnsemblBacteria; BAI29004; BAI29004; ECO103_0126.
DR   KEGG; eoh:ECO103_0126; -.
DR   HOGENOM; HOG000125184; -.
DR   KO; K01673; -.
DR   OMA; AWERGQD; -.
DR   BioCyc; ECOL585395:ECO103_RS00645-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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   InterPro; IPR036874; Carbonic_anhydrase_sf.
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; C8U1J6.
DR   SWISS-2DPAGE; C8U1J6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Lyase {ECO:0000256|RuleBase:RU003956};
KW   Zinc {ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   220 AA;  25097 MW;  48A9086BE9428452 CRC64;
     MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL
     FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL
     LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA
     YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK
//

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