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Database: UniProt
Entry: E8WKI5_GEOS8
LinkDB: E8WKI5_GEOS8
Original site: E8WKI5_GEOS8 
ID   E8WKI5_GEOS8            Unreviewed;       229 AA.
AC   E8WKI5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   OrderedLocusNames=GM18_0998 {ECO:0000313|EMBL:ADW12474.1};
OS   Geobacter sp. (strain M18).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW12474.1, ECO:0000313|Proteomes:UP000001442};
RN   [1] {ECO:0000313|EMBL:ADW12474.1, ECO:0000313|Proteomes:UP000001442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18 {ECO:0000313|EMBL:ADW12474.1,
RC   ECO:0000313|Proteomes:UP000001442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA   Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000943};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217}.
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DR   EMBL; CP002479; ADW12474.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8WKI5; -.
DR   STRING; 443143.GM18_0998; -.
DR   KEGG; geb:GM18_0998; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_053879_4_2_7; -.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000001442; 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   CDD; cd03378; beta_CA_cladeC; 1.
DR   Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
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:SF13; CARBONIC ANHYDRASE 2; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..229
FT                   /note="carbonic anhydrase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003233135"
SQ   SEQUENCE   229 AA;  23827 MW;  BFEFF614C1BA22DA CRC64;
     MKSSKVARRI AILATALAAT VGIAFASSEG AGITADQALQ KLMDGNTRYV ESKMSATALC
     DATARGKLAK SQHPYAIILS CSDSRVPPEI IFDQALGEVF VVRVAGNVAD PLVLGSVEYA
     AEHLGSPLIV VLGHERCGAV TATVEGGKPE GNIGAIVKAI APAAKKAKTN CKGRAKEEIV
     ECAVEINAKA VAAELPKKSK ILAHELKEGK IKIVAAKYDL DDGKVTLLK
//
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