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Database: UniProt
Entry: D6ZX76_BIFLJ
LinkDB: D6ZX76_BIFLJ
Original site: D6ZX76_BIFLJ 
ID   D6ZX76_BIFLJ            Unreviewed;       227 AA.
AC   D6ZX76;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   OrderedLocusNames=BLJ_0025 {ECO:0000313|EMBL:ADG99522.1};
OS   Bifidobacterium longum subsp. longum (strain JDM301).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=759350 {ECO:0000313|EMBL:ADG99522.1, ECO:0000313|Proteomes:UP000006740};
RN   [1] {ECO:0000313|EMBL:ADG99522.1, ECO:0000313|Proteomes:UP000006740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM301 {ECO:0000313|EMBL:ADG99522.1,
RC   ECO:0000313|Proteomes:UP000006740};
RX   PubMed=20525832; DOI=10.1128/JB.00538-10;
RA   Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA   Wang S., Guo X.K.;
RT   "Complete genome sequence of Bifidobacterium longum JDM301.";
RL   J. Bacteriol. 192:4076-4077(2010).
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; CP002010; ADG99522.1; -; Genomic_DNA.
DR   RefSeq; WP_013139965.1; NC_014169.1.
DR   AlphaFoldDB; D6ZX76; -.
DR   KEGG; bll:BLJ_0025; -.
DR   HOGENOM; CLU_053879_4_1_11; -.
DR   Proteomes; UP000006740; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  24900 MW;  6F5E90203B2B9B66 CRC64;
     MAQSDFEQES TANATWSRML QGNRRFAEGK PDHPWQDKET RQTLLDGQNP DAAVLSCSDS
     RVPPEIIFDQ GLGDLFTVRT AGQLIDSAVI ASLEYAVKKL HVSLICVLGH EHCGAIEAAE
     QELDDLMHTI TSEADGSLEA ADAMDDLDEH IAAAESIILR QAGMSVWQAR EAELDAHEDI
     ERVHVAHTIE TLVEQSPIIQ QALAADQLMI VGARYQLDTG KVEVLSF
//
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