ID   J7QWT3_METSZ            Unreviewed;       255 AA.
AC   J7QWT3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   OrderedLocusNames=BN69_3434 {ECO:0000313|EMBL:CCJ08885.1};
OS   Methylocystis sp. (strain SC2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ08885.1, ECO:0000313|Proteomes:UP000005263};
RN   [1] {ECO:0000313|EMBL:CCJ08885.1, ECO:0000313|Proteomes:UP000005263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:CCJ08885.1,
RC   ECO:0000313|Proteomes:UP000005263};
RX   PubMed=23045511; DOI=10.1128/JB.01446-12;
RA   Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT   "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT   Methanotroph with High-Affinity Methane Oxidation Potential.";
RL   J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ08885.1; -; Genomic_DNA.
DR   RefSeq; WP_014892911.1; NC_018485.1.
DR   AlphaFoldDB; J7QWT3; -.
DR   STRING; 187303.BN69_3434; -.
DR   KEGG; msc:BN69_3434; -.
DR   PATRIC; fig|187303.17.peg.3707; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_053879_4_2_5; -.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000005263; 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, ECO:0000313|EMBL:CCJ08885.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   REGION          39..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   255 AA;  27121 MW;  6C2C12DF396F1F67 CRC64;
     MCQACGFADI VHGGKMRRRA FVFGAATAGA LTVVANAHAQ GRKSQSKQAK QTSAPPKPDN
     VMTPDEAMAR LMEGNRRYQK GIAKRHDFIA EREALVGGQN PYAAILSCAD SRIAPEYAFD
     SSRGDLFVVR VAGNFANPDN IASMEYAVEV LKTPLILVLC HEACGAVKSA ISSIQDHTTL
     PGHLPSLVAA LAPAVKAVAG RPGDQLENAT MENARLGVET LKTATPLLSA AFNEKRFKIA
     SGIYRLGDGR VDLFA
//