CYNS_LACBS
ID CYNS_LACBS Reviewed; 165 AA.
AC B0DN41;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=LACBIDRAFT_174676;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547120; EDR03990.1; -; Genomic_DNA.
DR RefSeq; XP_001885245.1; XM_001885210.1.
DR AlphaFoldDB; B0DN41; -.
DR SMR; B0DN41; -.
DR STRING; 486041.B0DN41; -.
DR EnsemblFungi; EDR03990; EDR03990; LACBIDRAFT_174676.
DR GeneID; 6080877; -.
DR KEGG; lbc:LACBIDRAFT_174676; -.
DR HOGENOM; CLU_103452_1_0_1; -.
DR InParanoid; B0DN41; -.
DR OrthoDB; 1486663at2759; -.
DR Proteomes; UP000001194; 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..165
FT /note="Cyanate hydratase"
FT /id="PRO_0000403252"
FT ACT_SITE 106
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT ACT_SITE 109
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT ACT_SITE 132
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
SQ SEQUENCE 165 AA; 18218 MW; C88061E9A8BA1118 CRC64;
MSFASAPTVP TNTSHYADLP AASSALFQAK ARRGLTFDQI AKAIGKDEVW LAAAFYGQAR
FTEDELITVG EVLGIGSSEL VSQLGSHWWP NRGLGPMPPT DPVIYRLYES VLVYGHAIKA
VIHEKFGDGI MSMIDCKINV ERKEDPKGDR VLLTFDGKFL PYARW