CYNS_SORMK
ID CYNS_SORMK Reviewed; 164 AA.
AC D1ZHN6; B7FCD5; F7W0F4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 25-MAY-2022, entry version 55.
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=SMAC_03958;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ARG-104; GLU-107 AND SER-130.
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell; TISSUE=Mycelium;
RX PubMed=18796334; DOI=10.1016/j.fgb.2008.08.005;
RA Elleuche S., Poeggeler S.;
RT "A cyanase is transcriptionally regulated by arginine and involved in
RT cyanate decomposition in Sordaria macrospora.";
RL Fungal Genet. Biol. 45:1458-1469(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC ammonia and carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_03139,
CC ECO:0000269|PubMed:18796334}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for cyanate {ECO:0000269|PubMed:18796334};
CC Vmax=3163 nmol/min/mg enzyme {ECO:0000269|PubMed:18796334};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:18796334};
CC Temperature dependence:
CC Thermostable for 1 hour up to 60 degrees Celsius.
CC {ECO:0000269|PubMed:18796334};
CC -!- INDUCTION: Induced by cyanate and down-regulated by arginine.
CC {ECO:0000269|PubMed:18796334}.
CC -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000255|HAMAP-
CC Rule:MF_03139}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCC11254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CCC11254.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM773726; CAO79555.1; -; Genomic_DNA.
DR EMBL; CABT02000017; CCC11254.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; D1ZHN6; -.
DR SMR; D1ZHN6; -.
DR STRING; 771870.D1ZHN6; -.
DR EnsemblFungi; CCC11254; CCC11254; SMAC_03958.
DR eggNOG; ENOG502S3YJ; Eukaryota.
DR HOGENOM; CLU_168413_0_0_1; -.
DR InParanoid; D1ZHN6; -.
DR OrthoDB; 1486663at2759; -.
DR BRENDA; 4.2.1.104; 10681.
DR Proteomes; UP000001881; 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 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..164
FT /note="Cyanate hydratase"
FT /id="PRO_0000403267"
FT ACT_SITE 104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT MUTAGEN 104
FT /note="R->A,L: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:18796334"
FT MUTAGEN 107
FT /note="E->A,D: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:18796334"
FT MUTAGEN 130
FT /note="S->A,T: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:18796334"
SQ SEQUENCE 164 AA; 18115 MW; 42D695778FEE4471 CRC64;
MPEQQRLATL DSSIVSRLPA YSQSLFEAKT QKGLTFEAIA QHLGRSEVAV AGLFYGQVQA
SAEDVDKLSE LLSVPKEAIA AQMMGFPDRG RAGPMPPVEP LIYRLYEIVQ NYGYAFKAVM
NEKFGDGIMS AICFNTTVDK EVDETGAAWV VITLKGKWLP FTRF
