ID   CAH_PECAS               Reviewed;         244 AA.
AC   Q6DAJ6;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Carbonic anhydrase;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase;
DE   Flags: Precursor;
GN   Name=cah; OrderedLocusNames=ECA0257;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; BX950851; CAG73177.1; -; Genomic_DNA.
DR   RefSeq; WP_011091892.1; NC_004547.2.
DR   AlphaFoldDB; Q6DAJ6; -.
DR   SMR; Q6DAJ6; -.
DR   STRING; 218491.ECA0257; -.
DR   EnsemblBacteria; CAG73177; CAG73177; ECA0257.
DR   GeneID; 57207129; -.
DR   KEGG; eca:ECA0257; -.
DR   PATRIC; fig|218491.5.peg.258; -.
DR   eggNOG; COG3338; Bacteria.
DR   HOGENOM; CLU_039326_0_2_6; -.
DR   OMA; RMRMENN; -.
DR   OrthoDB; 1572675at2; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Lyase; Metal-binding; Periplasm; Reference proteome;
KW   Signal; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..244
FT                   /note="Carbonic anhydrase"
FT                   /id="PRO_0000042160"
FT   DOMAIN          23..244
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        84
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         195..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..199
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  26664 MW;  BAAC954DDD4EC1B1 CRC64;
     MKGKFSIALM LSACFSASAS DSVHWGYEGS GDPAHWGKLS PDFSLCETGK NQSPVNIQQA
     LNAQHDPLQL AFQSGTQQII NNGHTVQVNV SSGNTLLLDN ETFALQQFHF HAPSENEIDG
     KQFPLEGHFV YKNADGALTV IALMFQEGAA NPQLATAWQQ IPAHVDQAED VRTPIAIQAL
     LPTSLNYYRF SGSLTTPPCS EGIRWLVLDH PVTASAEQIN QFSSVMHHAN NRPIQPLNGR
     IIIH