ID   METX_YEAST              Reviewed;         649 AA.
AC   Q04533; D6W0K0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Putative cystathionine gamma-synthase YML082W;
DE            EC=2.5.1.48;
DE   AltName: Full=O-succinylhomoserine (thiol)-lyase;
GN   OrderedLocusNames=YML082W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
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., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-
CC       homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In
CC       the absence of thiol, catalyzes gamma-elimination to form 2-
CC       oxobutanoate, succinate and ammonia (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-
CC         cystathionine + succinate; Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661,
CC         ChEBI:CHEBI:58161; EC=2.5.1.48;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
CC   -!- MISCELLANEOUS: Present with 2810 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MET7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; Z46660; CAA86656.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09814.1; -; Genomic_DNA.
DR   PIR; S49644; S49644.
DR   RefSeq; NP_013628.1; NM_001182441.1.
DR   AlphaFoldDB; Q04533; -.
DR   SMR; Q04533; -.
DR   BioGRID; 35058; 43.
DR   DIP; DIP-5313N; -.
DR   IntAct; Q04533; 3.
DR   STRING; 4932.YML082W; -.
DR   iPTMnet; Q04533; -.
DR   MaxQB; Q04533; -.
DR   PaxDb; Q04533; -.
DR   PRIDE; Q04533; -.
DR   EnsemblFungi; YML082W_mRNA; YML082W; YML082W.
DR   GeneID; 854892; -.
DR   KEGG; sce:YML082W; -.
DR   SGD; S000004547; YML082W.
DR   VEuPathDB; FungiDB:YML082W; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   GeneTree; ENSGT00940000176383; -.
DR   HOGENOM; CLU_011302_1_0_1; -.
DR   InParanoid; Q04533; -.
DR   OMA; CSARFIN; -.
DR   BioCyc; YEAST:YML082W-MON; -.
DR   UniPathway; UPA00051; UER00077.
DR   PRO; PR:Q04533; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04533; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; ISS:SGD.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006790; P:sulfur compound metabolic process; ISS:SGD.
DR   GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Methionine biosynthesis; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..649
FT                   /note="Putative cystathionine gamma-synthase YML082W"
FT                   /id="PRO_0000114783"
FT   REGION          242..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         287
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         451
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   649 AA;  74313 MW;  FA952FBA0500BF6E CRC64;
     MVSAQVATEL GQPIPLDTQH AVSVCFPTWK SVISYVEKDP KVLGCLKSGY PRFWIHPSIQ
     KLRDILIEKY AKENETCFCF PSYRVAKRCR EYVRRKCAHR NGKVRILQLA TAKPINEEQK
     TWKRECKIAV VFVDGAYENI LKQYWQYTGE IISSRLAEYV LHELFMVEKK SSPAEEKEYI
     EMRYGRNLNF AFADRAKELI KKRIATKVID KDEHDEEENY HFLAGNQDEQ DFQDTFLDSS
     LNEANHGEDH DGGISGEVDS QEEPHNGLVS TIPPEPIEMS TIEEEQSVEE DAGRCALRVC
     PERDVFLFPS GMASIFTAHR LLLQWDSLRL NRSRNGSDVT SSPPNKKTVI FGFPYADTLH
     VLQEFNETYF LGEGDESSMK ELTKILHSGE QILAVFIETP SNPLLKMGNL LELKRLSELF
     GFFIIIDETV GGIVNIDGLP FADIVCSSLT KTFSGDSNVI GGSMVLNPQS RVYEFASRFM
     QLEDEYEDLL WCEDAIYLER NSRDFIARTI RINYSTEYLL DKILKPHVGE NKLFKKIYYP
     NLTSKETLTN YDMVRCKKEG GYGGLFSLTF HDEDHAAAFY DNLKLNKGPS LGTNFTLAFP
     YTLMTYYHEL DMAEKFGVER NLLRISVGLE SQSILGKIFQ EAIDKTVEI