ID A0A259UX52_9FIRM Unreviewed; 208 AA.
AC A0A259UX52;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
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 Name=icfA {ECO:0000313|EMBL:OZC22721.1};
GN ORFNames=SPACI_12670 {ECO:0000313|EMBL:OZC22721.1};
OS Sporomusa acidovorans DSM 3132.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC22721.1, ECO:0000313|Proteomes:UP000216052};
RN [1] {ECO:0000313|EMBL:OZC22721.1, ECO:0000313|Proteomes:UP000216052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC22721.1,
RC ECO:0000313|Proteomes:UP000216052};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OZC22721.1}.
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DR EMBL; LSLL01000038; OZC22721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259UX52; -.
DR STRING; 112900.SAMN04488499_102199; -.
DR Proteomes; UP000216052; 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; PS00704; PROK_CO2_ANHYDRASE_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000216052};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 208 AA; 23937 MW; 96C51A5B6896C8A3 CRC64;
MQRLLDGIVK FRRDDFENHR DLFKSLKSEQ KPHTLFITCS DSRVDPNLIT KTLPGELFII
RNIANLVPPY RETPEYVSTT SAIEYAVLSL GVENIIVCGH SHCGGCAACL GPAERLNNMP
HTKRWMELAI PVRDRILKEI AKDDIEARRW MMEQANVVEQ LKHLMGYPYI YEKTISGQLM
LSGWYYIIET GEVFIYDKNL GEFRLANG
//