ID I2DYP1_9BURK Unreviewed; 284 AA.
AC I2DYP1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN ORFNames=MYA_5424 {ECO:0000313|EMBL:AFJ89767.1};
OS Burkholderia sp. KJ006.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ89767.1, ECO:0000313|Proteomes:UP000010108};
RN [1] {ECO:0000313|EMBL:AFJ89767.1, ECO:0000313|Proteomes:UP000010108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ89767.1,
RC ECO:0000313|Proteomes:UP000010108};
RX PubMed=22843575; DOI=10.1128/JB.00821-12;
RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT Strain KJ006.";
RL J. Bacteriol. 194:4432-4433(2012).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU003956}.
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 ECO:0000256|RuleBase:RU003956};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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DR EMBL; CP003516; AFJ89767.1; -; Genomic_DNA.
DR AlphaFoldDB; I2DYP1; -.
DR KEGG; buk:MYA_5424; -.
DR PATRIC; fig|416344.3.peg.5518; -.
DR HOGENOM; CLU_053879_4_2_4; -.
DR Proteomes; UP000010108; Chromosome 3.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF76; CARBONIC ANHYDRASE; 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.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 284 AA; 30197 MW; ECF881998966AFA7 CRC64;
MHTALNTHSA RSKPAVVQCT HRHINQFNST GIKTNMCKSD TCKTATNHPA RRQFIRMAGV
SALGVAASGA SLTSFAATPD TRPLPKPLNA MSPDAAISRL KEGNARYVAG LMLRHDFAHE
RESLGTGQNP YAAVLSCADS RIAPEYAFDS ARGDLFAVRV AGNFVNDDVL GSLEYAVAVL
KTPVILVLGH DKCGAVSAAV NIETKGTIYP GKIQDLAMAM LPSVRQAQRA GGVPLDAAIA
QNVKDSVRHL SARSTIISGA KRDRKLKIIG GIYRLATGHV DFIV
//