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CYNS_PODAN
ID   CYNS_PODAN              Reviewed;         165 AA.
AC   B2B4S6; A0A090CCA2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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}; OrderedLocusNames=Pa_2_2300;
GN   ORFNames=PODANS_2_2300;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; CU640366; CAP72801.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP25200.1; -; Genomic_DNA.
DR   RefSeq; XP_001910976.1; XM_001910941.1.
DR   AlphaFoldDB; B2B4S6; -.
DR   SMR; B2B4S6; -.
DR   STRING; 5145.XP_001910976.1; -.
DR   EnsemblFungi; CAP72801; CAP72801; PODANS_2_2300.
DR   GeneID; 6195266; -.
DR   KEGG; pan:PODANSg8018; -.
DR   VEuPathDB; FungiDB:PODANS_2_2300; -.
DR   eggNOG; ENOG502S3YJ; Eukaryota.
DR   HOGENOM; CLU_103452_0_0_1; -.
DR   OrthoDB; 1486663at2759; -.
DR   Proteomes; UP000001197; Chromosome 2.
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..165
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_0000403264"
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;  18119 MW;  81227294CA10DA40 CRC64;
     MADSAPRLAA LDDSIVSRLP SYSQSLFAAK TAHELSFSAI AEHLGRSEVA VAALFYGQAT
     ASPEDITKLA ELLSLPEAQL RKDLGTGFPD RGRSGPMPPV EPLIYRLYEV VQNYGYAFKS
     VINEKFGDGI MSAICFDTKV EKETVEGADW VVITLRGKWL PFTRF
 
 
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