ID   CYNS_MAGO7              Reviewed;         162 AA.
AC   A4R2S1; G4MRW0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Cyanate hydratase {ECO:0000255|HAMAP-Rule:MF_03139};
DE            Short=Cyanase {ECO:0000255|HAMAP-Rule:MF_03139};
DE            EC=4.2.1.104 {ECO:0000255|HAMAP-Rule:MF_03139};
DE   AltName: Full=Cyanate hydrolase {ECO:0000255|HAMAP-Rule:MF_03139};
DE   AltName: Full=Cyanate lyase {ECO:0000255|HAMAP-Rule:MF_03139};
GN   Name=CYN1 {ECO:0000255|HAMAP-Rule:MF_03139}; ORFNames=MGG_02451;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC       ammonia and carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_03139}.
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_03139};
CC   -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03139}.
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DR   EMBL; CM001231; EHA56629.1; -; Genomic_DNA.
DR   RefSeq; XP_003709241.1; XM_003709193.1.
DR   AlphaFoldDB; A4R2S1; -.
DR   SMR; A4R2S1; -.
DR   STRING; 318829.MGG_02451T0; -.
DR   EnsemblFungi; MGG_02451T0; MGG_02451T0; MGG_02451.
DR   GeneID; 2681548; -.
DR   KEGG; mgr:MGG_02451; -.
DR   VEuPathDB; FungiDB:MGG_02451; -.
DR   eggNOG; ENOG502S3I5; Eukaryota.
DR   HOGENOM; CLU_103452_0_0_1; -.
DR   InParanoid; A4R2S1; -.
DR   OMA; YELVMIN; -.
DR   OrthoDB; 1486663at2759; -.
DR   Proteomes; UP000009058; 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   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   Gene3D; 3.30.1160.10; -; 1.
DR   HAMAP; MF_00535; Cyanate_hydrat; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
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; Reference proteome.
FT   CHAIN           1..162
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_0000403253"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
SQ   SEQUENCE   162 AA;  17939 MW;  8A7D6F9FEA48F948 CRC64;
     MAETRLASLD DSMASRLPVH SQTLFDAKTA KKLTFEAIAS KLGRSEVAVA GMFYGQVQAS
     GEDVEALSEL LGVPKESLSK MTNFPDRGRS GPMPPVEPLI YRLYEVVQNY GYSFKAVMNE
     KFGDGIMSAI CFQTNVEKEV DEQGATWAVI TLRGKWLPFT RF