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Database: UniProt
Entry: H0FBX1_9BURK
LinkDB: H0FBX1_9BURK
Original site: H0FBX1_9BURK 
ID   H0FBX1_9BURK            Unreviewed;       221 AA.
AC   H0FBX1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   ORFNames=KYC_21401 {ECO:0000313|EMBL:EHK64247.1};
OS   Achromobacter arsenitoxydans SY8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK64247.1, ECO:0000313|Proteomes:UP000003113};
RN   [1] {ECO:0000313|EMBL:EHK64247.1, ECO:0000313|Proteomes:UP000003113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8 {ECO:0000313|EMBL:EHK64247.1,
RC   ECO:0000313|Proteomes:UP000003113};
RX   PubMed=22328747; DOI=10.1128/JB.06667-11;
RA   Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT   "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT   Achromobacter arsenitoxydans SY8.";
RL   J. Bacteriol. 194:1243-1244(2012).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
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         ECO:0000256|RuleBase:RU003956};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK64247.1}.
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DR   EMBL; AGUF01000067; EHK64247.1; -; Genomic_DNA.
DR   RefSeq; WP_008166152.1; NZ_AGUF01000067.1.
DR   AlphaFoldDB; H0FBX1; -.
DR   STRING; 477184.KYC_21401; -.
DR   PATRIC; fig|477184.5.peg.4207; -.
DR   eggNOG; COG0288; Bacteria.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000003113; Unassembled WGS sequence.
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   CDD; cd00884; beta_CA_cladeB; 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:SF83; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   221 AA;  24633 MW;  C9AEF11D045D7606 CRC64;
     MRDIERLVGG FQRFQQQYYE DAPSLYQNLR EGQHPGTLLI GCCDSRVDPA MLLGCDPGDI
     FTVRNVANLV PPASKDRGLQ GVLAAIQFAV EQLQVSRIIV LGHAQCGGIR ALMERGIRRD
     GETDYLGRWM DIAEPARERV LQQMPDASKE ERRRACEQAS ILISLRNLED LPFVRRAVDA
     GSLTLHGWYF DLVAGALLAY SPRADTFLPI VCPLLTEPAL I
//
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