ID A0A1M6C348_9FIRM Unreviewed; 148 AA.
AC A0A1M6C348;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=SAMN02745751_00564 {ECO:0000313|EMBL:SHI55440.1};
OS Dethiosulfatibacter aminovorans DSM 17477.
OC Bacteria; Bacillota; Tissierellia; Dethiosulfatibacter.
OX NCBI_TaxID=1121476 {ECO:0000313|EMBL:SHI55440.1, ECO:0000313|Proteomes:UP000184052};
RN [1] {ECO:0000313|EMBL:SHI55440.1, ECO:0000313|Proteomes:UP000184052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17477 {ECO:0000313|EMBL:SHI55440.1,
RC ECO:0000313|Proteomes:UP000184052};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQZL01000005; SHI55440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6C348; -.
DR STRING; 1121476.SAMN02745751_00564; -.
DR Proteomes; UP000184052; 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 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: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 Reference proteome {ECO:0000313|Proteomes:UP000184052};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 148 AA; 17175 MW; 43C6BC8FE972EA97 CRC64;
MPGELFTINN IANIVPPYCD ALEYVATTSA IEYAINVLEV ENVIVCGHSN CGGCNIDHNS
FESLERLPLM RKWLELIKPI KMSSSNDTWK RMVEQNNVIE QLKHLMTYPY IYEKVKTENL
KLSGWYYQIE TGEIFIYDEG AKEFQLRN
//
