ID B8DV51_BIFA0 Unreviewed; 225 AA.
AC B8DV51;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN Name=icfA {ECO:0000313|EMBL:ACL28352.1};
GN OrderedLocusNames=BLA_0049 {ECO:0000313|EMBL:ACL28352.1};
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL28352.1, ECO:0000313|Proteomes:UP000002456};
RN [1] {ECO:0000313|EMBL:ACL28352.1, ECO:0000313|Proteomes:UP000002456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011 {ECO:0000313|EMBL:ACL28352.1,
RC ECO:0000313|Proteomes:UP000002456};
RX PubMed=19011029; DOI=10.1128/JB.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
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; CP001213; ACL28352.1; -; Genomic_DNA.
DR RefSeq; WP_012619617.1; NC_011835.1.
DR AlphaFoldDB; B8DV51; -.
DR STRING; 442563.BLA_0049; -.
DR GeneID; 66532425; -.
DR KEGG; bla:BLA_0049; -.
DR PATRIC; fig|442563.4.peg.53; -.
DR HOGENOM; CLU_053879_4_1_11; -.
DR Proteomes; UP000002456; 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 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, ECO:0000313|EMBL:ACL28352.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002456};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 225 AA; 25111 MW; CDA15E508577B3C3 CRC64;
MTDSTQETTA NSTWSRMLAG NRRFAEGNAE HPWRDKETRE SLIDTQNPDA AVLSCSDSRV
PPEIIFDAGL GDMFTVRTAG EMLDQAVLQT LEYAVSSLHV SLLVVLSHQH CAAVAQAEKE
LDALTEHLTH EITDAQERER IMEDLDEVIA SSSSEFLKNI GISVWQARMA GLDSRDDYEQ
VHIAHTIEQL VTSSEMIRDA LAHERLMIVG ARYRLDTGLV EVLSF
//
