ID Q8G6M3_BIFLO Unreviewed; 227 AA.
AC Q8G6M3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
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:AAN24439.1};
GN OrderedLocusNames=BL0616 {ECO:0000313|EMBL:AAN24439.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24439.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN24439.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24439.1; -; Genomic_DNA.
DR RefSeq; NP_695803.1; NC_004307.2.
DR RefSeq; WP_011068585.1; NC_004307.2.
DR AlphaFoldDB; Q8G6M3; -.
DR STRING; 206672.BL0616; -.
DR EnsemblBacteria; AAN24439; AAN24439; BL0616.
DR KEGG; blo:BL0616; -.
DR PATRIC; fig|206672.9.peg.1351; -.
DR HOGENOM; CLU_053879_4_1_11; -.
DR OrthoDB; 9797527at2; -.
DR PhylomeDB; Q8G6M3; -.
DR Proteomes; UP000000439; 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 CDD; cd03378; beta_CA_cladeC; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 227 AA; 24826 MW; 7D54413DAC6F0D06 CRC64;
MAQSDFEQES TANATWSRML QGNRRFAEGK PDHPWQDQET RQTLLDGQNP DAAVLSCSDS
RVPPEIIFDQ GLGDLFTVRT AGQLIDSAVI ASLEYAVKKL HVSLICVLGH EHCGAIEAAE
QELDDLMHTI TSEADGSLEA ADAMDGLDEH IAAAESIILR QAGMSVWQAR EAELDAHEDI
ERVHVAHIIE TLVEQSPVIQ QALAADKLMI VGARYQLDSG KVEVLSF
//
