ID   CYNS_BURPS              Reviewed;         156 AA.
AC   Q63QS4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cyanate hydratase {ECO:0000255|HAMAP-Rule:MF_00535};
DE            Short=Cyanase {ECO:0000255|HAMAP-Rule:MF_00535};
DE            EC=4.2.1.104 {ECO:0000255|HAMAP-Rule:MF_00535};
DE   AltName: Full=Cyanate hydrolase {ECO:0000255|HAMAP-Rule:MF_00535};
DE   AltName: Full=Cyanate lyase {ECO:0000255|HAMAP-Rule:MF_00535};
GN   Name=cynS {ECO:0000255|HAMAP-Rule:MF_00535}; OrderedLocusNames=BPSL2950;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC       ammonia and carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_00535}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+);
CC         Xref=Rhea:RHEA:11120, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:29195;
CC         EC=4.2.1.104; Evidence={ECO:0000255|HAMAP-Rule:MF_00535};
CC   -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00535}.
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DR   EMBL; BX571965; CAH36960.1; -; Genomic_DNA.
DR   RefSeq; WP_004522069.1; NZ_CP009538.1.
DR   RefSeq; YP_109544.1; NC_006350.1.
DR   AlphaFoldDB; Q63QS4; -.
DR   SMR; Q63QS4; -.
DR   STRING; 272560.BPSL2950; -.
DR   EnsemblBacteria; CAH36960; CAH36960; BPSL2950.
DR   GeneID; 56528247; -.
DR   KEGG; bps:BPSL2950; -.
DR   PATRIC; fig|272560.51.peg.2329; -.
DR   eggNOG; COG1513; Bacteria.
DR   OMA; YELVMIN; -.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0008824; F:cyanate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009439; P:cyanate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00559; Cyanase_C; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   Gene3D; 3.30.1160.10; -; 1.
DR   HAMAP; MF_00535; Cyanate_hydrat; 1.
DR   InterPro; IPR008076; Cyanase.
DR   InterPro; IPR003712; Cyanate_lyase_C.
DR   InterPro; IPR036581; Cyanate_lyase_C_sf.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   PANTHER; PTHR34186; PTHR34186; 1.
DR   Pfam; PF02560; Cyanate_lyase; 1.
DR   PIRSF; PIRSF001263; Cyanate_hydratas; 1.
DR   PRINTS; PR01693; CYANASE.
DR   SMART; SM01116; Cyanate_lyase; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF55234; SSF55234; 1.
DR   TIGRFAMs; TIGR00673; cynS; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..156
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_1000051473"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
SQ   SEQUENCE   156 AA;  16932 MW;  556CAF024D8B9894 CRC64;
     MTQSQHSQSA REALAERIVE AKTRKNLTFE QINEGTGLSV AFTTAALLGQ HPLPADAARV
     VAAKLDLDDD AQRLLQTIPV RGSIPGGVPT DPTIYRFYEI VQVYGSTLKA LIHEQFGDGI
     VSAINFKLDI KKVDDPEGGS RAVITLDGKY LPTKPF