ID   CYNS_BURCJ              Reviewed;         156 AA.
AC   B4EJC2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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};
GN   OrderedLocusNames=BceJ2315_38620; ORFNames=BCAM0401;
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX   PubMed=18931103; DOI=10.1128/jb.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
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; AM747721; CAR54257.1; -; Genomic_DNA.
DR   RefSeq; WP_006485483.1; NC_011001.1.
DR   AlphaFoldDB; B4EJC2; -.
DR   SMR; B4EJC2; -.
DR   STRING; 216591.BCAM0401; -.
DR   EnsemblBacteria; CAR54257; CAR54257; BCAM0401.
DR   KEGG; bcj:BCAM0401; -.
DR   eggNOG; COG1513; Bacteria.
DR   HOGENOM; CLU_103452_1_1_4; -.
DR   OMA; YELVMIN; -.
DR   OrthoDB; 1506439at2; -.
DR   BioCyc; BCEN216591:G1G1V-4356-MON; -.
DR   Proteomes; UP000001035; Chromosome 2.
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.
FT   CHAIN           1..156
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_1000128222"
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;  16931 MW;  C2C4E8BCE22D885E CRC64;
     MIQSQHSQTA RHALAETVVL AKARKNLSFA QLTDGTGLSE AFVTAALLGQ HALPADAARI
     VADKLGLDDD AVLLLQTIPL RGSIDDRVPT DPTIYRFYEM LQVYGTTLKA LVHEKFGDGI
     ISAINFRLDV KKVDDPEGGS RAVITLDGKY LPTKPF