(data stored in ACNUC10821 zone)

SWISSPROT: C8U233_ECO10

ID   C8U233_ECO10            Unreviewed;       156 AA.
AC   C8U233;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Cyanate hydratase {ECO:0000256|HAMAP-Rule:MF_00535};
DE            Short=Cyanase {ECO:0000256|HAMAP-Rule:MF_00535};
DE            EC=4.2.1.104 {ECO:0000256|HAMAP-Rule:MF_00535};
DE   AltName: Full=Cyanate hydrolase {ECO:0000256|HAMAP-Rule:MF_00535};
DE   AltName: Full=Cyanate lyase {ECO:0000256|HAMAP-Rule:MF_00535};
GN   Name=cynS {ECO:0000256|HAMAP-Rule:MF_00535,
GN   ECO:0000313|EMBL:BAI29191.1};
GN   OrderedLocusNames=ECO103_0322 {ECO:0000313|EMBL:BAI29191.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29191.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29191.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to
CC       produce ammonia and carbon dioxide. {ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-Rule:MF_00535};
CC   -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00535}.
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DR   EMBL; AP010958; BAI29191.1; -; Genomic_DNA.
DR   RefSeq; WP_000616241.1; NC_013353.1.
DR   SMR; C8U233; -.
DR   EnsemblBacteria; BAI29191; BAI29191; ECO103_0322.
DR   KEGG; eoh:ECO103_0322; -.
DR   HOGENOM; HOG000043436; -.
DR   KO; K01725; -.
DR   OMA; ITMSGKF; -.
DR   BioCyc; ECOL585395:ECO103_RS01685-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0008824; F:cyanate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009439; P:cyanate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00559; Cyanase_C; 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;
DR   PRODOM; C8U233.
DR   SWISS-2DPAGE; C8U233.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000313|EMBL:BAI29191.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00535}.
FT   DOMAIN       83    156       Cyanate_lyase. {ECO:0000259|SMART:
FT                                SM01116}.
FT   ACT_SITE     96     96       {ECO:0000256|HAMAP-Rule:MF_00535}.
FT   ACT_SITE     99     99       {ECO:0000256|HAMAP-Rule:MF_00535}.
FT   ACT_SITE    122    122       {ECO:0000256|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
//

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