CYNS_COPC7
ID CYNS_COPC7 Reviewed; 151 AA.
AC A8NV38;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 60.
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=CC1G_06180;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000004; EAU85164.2; -; Genomic_DNA.
DR RefSeq; XP_001836593.2; XM_001836541.2.
DR AlphaFoldDB; A8NV38; -.
DR SMR; A8NV38; -.
DR STRING; 5346.XP_001836593.2; -.
DR EnsemblFungi; EAU85164; EAU85164; CC1G_06180.
DR GeneID; 6013139; -.
DR KEGG; cci:CC1G_06180; -.
DR VEuPathDB; FungiDB:CC1G_06180; -.
DR eggNOG; ENOG502S3YJ; Eukaryota.
DR HOGENOM; CLU_103452_1_0_1; -.
DR InParanoid; A8NV38; -.
DR OMA; YELVMIN; -.
DR OrthoDB; 1486663at2759; -.
DR Proteomes; UP000001861; 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 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; Reference proteome.
FT CHAIN 1..151
FT /note="Cyanate hydratase"
FT /id="PRO_0000403249"
FT ACT_SITE 92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT ACT_SITE 95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT ACT_SITE 118
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
SQ SEQUENCE 151 AA; 16876 MW; 9EA5134D27622159 CRC64;
MTPAVSPAHT VLFEAKARKG ISFEQIGKAI GRDEVWVASA FYGQAKFNEE ELKKLSEVLE
ISSAQIVKEL GDQWFPNRGL GPVPPSDPVI YRLFEGVLVY GHPIKAIIHE KFGDGIMSMI
DCNINVERKP DPKGDRVVVT FDGKFLPYSK W