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Database: UniProt
Entry: P53206
LinkDB: P53206
Original site: P53206 
ID   CYSK_YEAST              Reviewed;         393 AA.
AC   P53206; D6VUE8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   01-MAY-2013, entry version 105.
DE   RecName: Full=Putative cysteine synthase;
DE            Short=CSase;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE            Short=OAS-TL;
DE   AltName: Full=O-acetylserine sulfhydrylase;
GN   OrderedLocusNames=YGR012W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(SICI)1097-0061(19970915)13:11<1077::AID-YEA152>3.3.CO;2-P;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- CATALYTIC ACTIVITY: O(3)-acetyl-L-serine + H(2)S = L-cysteine +
CC       acetate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
CC       cysteine from L-serine: step 2/2.
CC   -!- MISCELLANEOUS: Present with 4650 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family.
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DR   EMBL; Z72797; CAA96995.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08109.1; -; Genomic_DNA.
DR   PIR; S64303; S64303.
DR   RefSeq; NP_011526.1; NM_001181141.1.
DR   ProteinModelPortal; P53206; -.
DR   SMR; P53206; 42-372.
DR   IntAct; P53206; 1.
DR   MINT; MINT-2492937; -.
DR   STRING; 4932.YGR012W; -.
DR   PaxDb; P53206; -.
DR   PeptideAtlas; P53206; -.
DR   EnsemblFungi; YGR012W; YGR012W; YGR012W.
DR   GeneID; 852895; -.
DR   KEGG; sce:YGR012W; -.
DR   CYGD; YGR012w; -.
DR   SGD; S000003244; YGR012W.
DR   eggNOG; COG0031; -.
DR   GeneTree; ENSGT00700000105450; -.
DR   HOGENOM; HOG000217393; -.
DR   KO; K01738; -.
DR   OMA; VAPAYGC; -.
DR   OrthoDB; EOG45MRFC; -.
DR   UniPathway; UPA00136; UER00200.
DR   NextBio; 972565; -.
DR   ArrayExpress; P53206; -.
DR   Genevestigator; P53206; -.
DR   GermOnline; YGR012W; Saccharomyces cerevisiae.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0004124; F:cysteine synthase activity; ISS:SGD.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   InterPro; IPR001216; Cys_synth_BS.
DR   InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN         1    393       Putative cysteine synthase.
FT                                /FTId=PRO_0000167130.
FT   REGION      230    234       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     338    338       Pyridoxal phosphate (By similarity).
FT   MOD_RES      86     86       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   393 AA;  42801 MW;  76C73396D77B69AC CRC64;
     MSCSQNKTSV SLAWRECISI ASVLIGAYAS YKYYKLFKTR DIPRPKEGVE ELIGNTPLVK
     IRSLTKATGV NIYAKLELCN PAGSAKDRVA LNIIKTAEEL GELVRGEPGW VFEGTSGSTG
     ISIAVVCNAL GYRAHISLPD DTSLEKLALL ESLGATVNKV KPASIVDPNQ YVNAAKKACN
     ELKKSGNGIR AVFADQFENE ANWKVHYQTT GPEIAHQTKG NIDAFIAGCG TGGTITGVAK
     FLKERAKIPC HVVLADPQGS GFYNRVNYGV MYDYVEKEGT RRRHQVDTIV EGIGLNRITH
     NFHMGEKFID ESIRVNDNQA IRMAKYLSVN DGLFVGSSTA INAVAAIQVA KTLPHGSNIV
     IIACDSGSRH LSKFWKEAKE IDHDVSLEEV INI
//
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