ID Q57T84_SALCH Unreviewed; 237 AA.
AC Q57T84;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=yadF {ECO:0000313|EMBL:AAX64077.1};
GN OrderedLocusNames=SCH_0171 {ECO:0000313|EMBL:AAX64077.1};
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX64077.1, ECO:0000313|Proteomes:UP000000538};
RN [1] {ECO:0000313|EMBL:AAX64077.1, ECO:0000313|Proteomes:UP000000538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67 {ECO:0000313|EMBL:AAX64077.1,
RC ECO:0000313|Proteomes:UP000000538};
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA Lee Y.S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64077.1; -; Genomic_DNA.
DR AlphaFoldDB; Q57T84; -.
DR KEGG; sec:SCH_0171; -.
DR HOGENOM; CLU_053879_3_0_6; -.
DR Proteomes; UP000000538; Chromosome.
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; cd00883; beta_CA_cladeA; 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: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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 237 AA; 26774 MW; F81EFEAABCF25251 CRC64;
MPYISPTHLF GYRSLTSMKD IDTLISNNAL WSKMLVEEDP GFFEKLAQAQ KPRFLWIGCS
DSRVPAERLT GLEPGELFVH RNVANLVIHT DLNCLSVVQY AVDVLEVEHI IICGHSGCGG
IKAAVENPEL GLINNWLLHI RDIWLKHSSL LGKMPEEQRL DALYELNVME QVYNLGHSTI
MQSAWKRGQN VTIHGWAYSI NDGLLRDLDV TATNRETLEN GYHKGISALS LKYIPHQ
//
