ID   CYNS_ECOLC              Reviewed;         156 AA.
AC   B1J0T9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=EcolC_3285;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 /
RC   Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA78907.1; -; Genomic_DNA.
DR   RefSeq; WP_000616249.1; NZ_MTFT01000010.1.
DR   AlphaFoldDB; B1J0T9; -.
DR   SMR; B1J0T9; -.
DR   KEGG; ecl:EcolC_3285; -.
DR   HOGENOM; CLU_103452_1_1_6; -.
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; 3.30.1160.10; Cyanate lyase, C-terminal domain; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR048564; CYNS_N.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   NCBIfam; TIGR00673; cynS; 1.
DR   PANTHER; PTHR34186; CYANATE HYDRATASE; 1.
DR   PANTHER; PTHR34186:SF2; CYANATE HYDRATASE; 1.
DR   Pfam; PF02560; Cyanate_lyase; 1.
DR   Pfam; PF21291; CYNS_N; 1.
DR   PIRSF; PIRSF001263; Cyanate_hydratas; 1.
DR   PRINTS; PR01693; CYANASE.
DR   SMART; SM01116; Cyanate_lyase; 1.
DR   SUPFAM; SSF55234; Cyanase C-terminal domain; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..156
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_1000081862"
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;  17054 MW;  63AA586490ED4D3D CRC64;
     MIQSQINRNI RLDLADAILL SKAKKDLSFA EIADGTGLAE AFVTEALLGQ QALPADAARL
     VGAKLDLDED SILLLQMIPL RGCIDDRIPT DPTMYRFYEM LQVYGTTLKA LVHEKFGDGI
     ISAINFKLDV KKVADPEGGE CAVITLDGKY LPTKPF
//