ID   MTCA1_MYCTO             Reviewed;         163 AA.
AC   P9WPJ6; L0T7U0; P64797; Q10612;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Beta-carbonic anhydrase 1;
DE            Short=Beta-CA 1;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase 1;
DE   AltName: Full=mtCA 1;
GN   Name=mtcA1; Synonyms=canA; OrderedLocusNames=MT1322;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC       bicarbonate. {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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45583.1; -; Genomic_DNA.
DR   PIR; H70771; H70771.
DR   RefSeq; WP_003406616.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPJ6; -.
DR   SMR; P9WPJ6; -.
DR   EnsemblBacteria; AAK45583; AAK45583; MT1322.
DR   GeneID; 45425256; -.
DR   KEGG; mtc:MT1322; -.
DR   PATRIC; fig|83331.31.peg.1428; -.
DR   HOGENOM; CLU_084253_1_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
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; PTHR43175; PTHR43175; 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; Zinc.
FT   CHAIN           1..163
FT                   /note="Beta-carbonic anhydrase 1"
FT                   /id="PRO_0000426940"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   163 AA;  18189 MW;  DDD342B7DBFE5AA0 CRC64;
     MTVTDDYLAN NVDYASGFKG PLPMPPSKHI AIVACMDARL DVYRMLGIKE GEAHVIRNAG
     CVVTDDVIRS LAISQRLLGT REIILLHHTD CGMLTFTDDD FKRAIQDETG IRPTWSPESY
     PDAVEDVRQS LRRIEVNPFV TKHTSLRGFV FDVATGKLNE VTP