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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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