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BCA1_CAEBR
ID   BCA1_CAEBR              Reviewed;         270 AA.
AC   A8XKV0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Beta carbonic anhydrase 1;
DE            EC=4.2.1.1;
GN   Name=bca-1 {ECO:0000312|EMBL:CAP33274.2}; ORFNames=CBG14861;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP33274.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP33274.2};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250}.
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; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P45148};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P45148};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000255}.
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DR   EMBL; HE600983; CAP33274.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XKV0; -.
DR   SMR; A8XKV0; -.
DR   STRING; 6238.CBG14861; -.
DR   EnsemblMetazoa; CBG14861.1; CBG14861.1; WBGene00035244.
DR   WormBase; CBG14861; CBP35478; WBGene00035244; Cbr-bca-1.
DR   eggNOG; KOG1578; Eukaryota.
DR   HOGENOM; CLU_053879_5_3_1; -.
DR   InParanoid; A8XKV0; -.
DR   OMA; PEDQDGP; -.
DR   OrthoDB; 1136193at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.40.1050.10; -; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; PTHR11002; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; SSF53056; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..270
FT                   /note="Beta carbonic anhydrase 1"
FT                   /id="PRO_0000374065"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P45148"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P45148"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P45148"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P45148"
SQ   SEQUENCE   270 AA;  30739 MW;  5D2088C567CEF150 CRC64;
     MNRIIRGVIQ YNQKIKAGLV KQFEHVSDHP NPTAVMFTCM DSRMLPTRFT QSAVGDMFVV
     RNAGNMIPAA PNYGSYSEVS INTEPAALEL AVKRGKIRHV VVCGHSDCKA MNTLYQLHQC
     PTKFDVSSPM DQWLRRNGFE SMKKLNERLH IGPKTMKFES EVAPSQSFEA IIDPMEKWSA
     EDKLSQINVL QQIMNISTHE FLKDYLEAGN LHLHGAWFNI YDGEVFLFSK DRKRFVVIDE
     KTVPSLSAEL ERRCPLPEDK AGDVVIQNLH
 
 
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