ID   CYNS_PYRTR              Reviewed;         162 AA.
AC   B2WIX9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 54.
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=PTRG_09938;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDU42989.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DS231626; EDU42989.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001940270.1; XM_001940235.1.
DR   AlphaFoldDB; B2WIX9; -.
DR   SMR; B2WIX9; -.
DR   STRING; 45151.EDU42989; -.
DR   GeneID; 6348236; -.
DR   eggNOG; ENOG502S3YJ; Eukaryota.
DR   InParanoid; B2WIX9; -.
DR   OrthoDB; 1486663at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
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_0000403265"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
SQ   SEQUENCE   162 AA;  18120 MW;  70F01970D5059066 CRC64;
     MAQHPIATLN EELVPRLPPS SPTLFEAKKK KNLSFEAIAK HVGRDEVAIA ALFYGQAMAS
     AQDIKKLSEI LDIDAGMLES QLSGFPNRGS TLDMPPKDPT IYRLYEIVQN YGQAYKAVLH
     EKFGDGIMSA ISFSTKIEKE TDDKGEWAKI TLRGKWLPYS RF