ID   CYNS_ECO7I              Reviewed;         156 AA.
AC   B7NK15;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=ECIAI39_0338;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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; CU928164; CAR16478.1; -; Genomic_DNA.
DR   RefSeq; WP_000616241.1; NC_011750.1.
DR   RefSeq; YP_002406380.1; NC_011750.1.
DR   AlphaFoldDB; B7NK15; -.
DR   SMR; B7NK15; -.
DR   STRING; 585057.ECIAI39_0338; -.
DR   EnsemblBacteria; CAR16478; CAR16478; ECIAI39_0338.
DR   GeneID; 66671356; -.
DR   KEGG; ect:ECIAI39_0338; -.
DR   PATRIC; fig|585057.6.peg.365; -.
DR   HOGENOM; CLU_103452_1_1_6; -.
DR   OMA; YELVMIN; -.
DR   Proteomes; UP000000749; Chromosome.
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_1000128224"
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;  17033 MW;  829E903B262F230C CRC64;
     MIQSQINRNI RLDLADAILL SKAKKDLSFA EIADGTGLAE AFVTAALLGQ QALPADAARL
     VGAKLDLDED AILLLQMIPL RGCIDDRIPT DPTMYRFYEM LQVYGTTLKA LVHEKFGDGI
     ISAINFKLDV KKVADPEGGE RAVITLDGKY LPTKPF