CYNS_BURMA
ID CYNS_BURMA Reviewed; 156 AA.
AC Q62H08;
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=BMA2466;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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; CP000010; AAU49682.1; -; Genomic_DNA.
DR RefSeq; WP_004194284.1; NC_006348.1.
DR RefSeq; YP_104012.1; NC_006348.1.
DR AlphaFoldDB; Q62H08; -.
DR SMR; Q62H08; -.
DR STRING; 243160.BMA2466; -.
DR EnsemblBacteria; AAU49682; AAU49682; BMA2466.
DR GeneID; 56594198; -.
DR KEGG; bma:BMA2466; -.
DR PATRIC; fig|243160.12.peg.2543; -.
DR eggNOG; COG1513; Bacteria.
DR HOGENOM; CLU_103452_1_1_4; -.
DR OMA; YELVMIN; -.
DR Proteomes; UP000006693; 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.
FT CHAIN 1..156
FT /note="Cyanate hydratase"
FT /id="PRO_1000051469"
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; 16958 MW; 457DA27F20E7E894 CRC64;
MTQSQHSQSP REALAERIVE AKTRKNLTFE QINEGTGLSV AFTTAALLGQ HPLPADAARV
VAAKLDLDDD AQRLLQTIPV RGSIPGGVPT DPTIYRFYEI VQVYGSTLKA LIHEQFGDGI
VSAINFKLDI KKVDDPEGGS RAVITLDGKY LPTKPF
