MTCA2_MYCTU
ID MTCA2_MYCTU Reviewed; 207 AA.
AC P9WPJ9; L0TFY5; O53573; Q7D582;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Carbonic anhydrase 2;
DE Short=Beta-CA 2;
DE EC=4.2.1.1 {ECO:0000269|PubMed:15753099};
DE AltName: Full=Carbonate dehydratase 2;
DE AltName: Full=mtCA 2;
GN Name=mtcA2; Synonyms=canB, cynT; OrderedLocusNames=Rv3588c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NOMENCLATURE.
RX PubMed=19317447; DOI=10.1021/jm9000488;
RA Minakuchi T., Nishimori I., Vullo D., Scozzafava A., Supuran C.T.;
RT "Molecular cloning, characterization, and inhibition studies of the Rv1284
RT beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides
RT and a sulfamate.";
RL J. Med. Chem. 52:2226-2232(2009).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=19438226; DOI=10.1021/jm9004016;
RA Guzel O., Maresca A., Scozzafava A., Salman A., Balaban A.T., Supuran C.T.;
RT "Discovery of low nanomolar and subnanomolar inhibitors of the
RT mycobacterial beta-carbonic anhydrases Rv1284 and Rv3273.";
RL J. Med. Chem. 52:4063-4067(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-207 IN COMPLEX WITH ZINC ION,
RP FUNCTION AS AN CARBONIC ANHYDRASE, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15753099; DOI=10.1074/jbc.m414348200;
RA Suarez Covarrubias A., Larsson A.M., Hogbom M., Lindberg J., Bergfors T.,
RA Bjorkelid C., Mowbray S.L., Unge T., Jones T.A.;
RT "Structure and function of carbonic anhydrases from Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 280:18782-18789(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-207 IN COMPLEX WITH ZINC ION,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16321983; DOI=10.1074/jbc.m510756200;
RA Covarrubias A.S., Bergfors T., Jones T.A., Hogbom M.;
RT "Structural mechanics of the pH-dependent activity of beta-carbonic
RT anhydrase from Mycobacterium tuberculosis.";
RL J. Biol. Chem. 281:4993-4999(2006).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC bicarbonate. {ECO:0000269|PubMed:15753099}.
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:0000269|PubMed:15753099};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15753099, ECO:0000269|PubMed:16321983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15753099,
CC ECO:0000269|PubMed:16321983};
CC -!- ACTIVITY REGULATION: Inhibited by sulfonamides and sulfamates.
CC {ECO:0000269|PubMed:19438226}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at pH 8.4 and inactive at pH 7.5.
CC {ECO:0000269|PubMed:16321983};
CC -!- SUBUNIT: Homotetramer at pH 8.4 and homodimer at pH 7.4.
CC {ECO:0000269|PubMed:15753099, ECO:0000269|PubMed:16321983}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46411.1; -; Genomic_DNA.
DR PIR; E70804; E70804.
DR RefSeq; NP_218105.1; NC_000962.3.
DR RefSeq; WP_003419492.1; NZ_NVQJ01000014.1.
DR PDB; 1YM3; X-ray; 1.75 A; A=2-207.
DR PDB; 2A5V; X-ray; 2.20 A; A/B/C/D=2-207.
DR PDBsum; 1YM3; -.
DR PDBsum; 2A5V; -.
DR AlphaFoldDB; P9WPJ9; -.
DR SMR; P9WPJ9; -.
DR STRING; 83332.Rv3588c; -.
DR BindingDB; P9WPJ9; -.
DR ChEMBL; CHEMBL6068; -.
DR DrugCentral; P9WPJ9; -.
DR PaxDb; P9WPJ9; -.
DR DNASU; 887836; -.
DR GeneID; 45427576; -.
DR GeneID; 887836; -.
DR KEGG; mtu:Rv3588c; -.
DR TubercuList; Rv3588c; -.
DR eggNOG; COG0288; Bacteria.
DR OMA; GHEGCGA; -.
DR PhylomeDB; P9WPJ9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
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.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..207
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000396117"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15753099,
FT ECO:0000269|PubMed:16321983, ECO:0007744|PDB:1YM3,
FT ECO:0007744|PDB:2A5V"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15753099,
FT ECO:0007744|PDB:1YM3"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15753099,
FT ECO:0000269|PubMed:16321983, ECO:0007744|PDB:1YM3,
FT ECO:0007744|PDB:2A5V"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15753099,
FT ECO:0000269|PubMed:16321983, ECO:0007744|PDB:1YM3,
FT ECO:0007744|PDB:2A5V"
FT HELIX 6..22
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:2A5V"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:2A5V"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1YM3"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:1YM3"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:1YM3"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:1YM3"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1YM3"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1YM3"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1YM3"
SQ SEQUENCE 207 AA; 21792 MW; 60BE85FA14847FEC CRC64;
MPNTNPVAAW KALKEGNERF VAGRPQHPSQ SVDHRAGLAA GQKPTAVIFG CADSRVAAEI
IFDQGLGDMF VVRTAGHVID SAVLGSIEYA VTVLNVPLIV VLGHDSCGAV NAALAAINDG
TLPGGYVRDV VERVAPSVLL GRRDGLSRVD EFEQRHVHET VAILMARSSA ISERIAGGSL
AIVGVTYQLD DGRAVLRDHI GNIGEEV
