MET7_YEAST
ID MET7_YEAST Reviewed; 639 AA.
AC P47164; D6VWU8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0000303|PubMed:10821189};
DE EC=2.5.1.48 {ECO:0000305|PubMed:10821189};
DE AltName: Full=O-succinylhomoserine (thiol)-lyase {ECO:0000303|PubMed:10821189};
DE AltName: Full=Sulfur transfer protein 2 {ECO:0000303|PubMed:10821189};
GN Name=STR2 {ECO:0000303|PubMed:10821189}; OrderedLocusNames=YJR130C;
GN ORFNames=J2063;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10821189; DOI=10.1007/s004380051199;
RA Hansen J., Johannesen P.F.;
RT "Cysteine is essential for transcriptional regulation of the sulfur
RT assimilation genes in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 263:535-542(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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).
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. {ECO:0000269|PubMed:10821189}.
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 Evidence={ECO:0000305|PubMed:10821189};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
CC {ECO:0000305|PubMed:10821189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Leads to a clear growth defect on medium
CC containing cysteine or glutathione as sole sulfur source.
CC {ECO:0000269|PubMed:10821189}.
CC -!- MISCELLANEOUS: Present with 2070 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; Z49630; CAA89661.1; -; Genomic_DNA.
DR EMBL; AY692979; AAT92998.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08914.1; -; Genomic_DNA.
DR PIR; S57153; S57153.
DR RefSeq; NP_012664.1; NM_001181788.1.
DR AlphaFoldDB; P47164; -.
DR SMR; P47164; -.
DR BioGRID; 33885; 109.
DR DIP; DIP-5049N; -.
DR IntAct; P47164; 1.
DR STRING; 4932.YJR130C; -.
DR iPTMnet; P47164; -.
DR MaxQB; P47164; -.
DR PaxDb; P47164; -.
DR PRIDE; P47164; -.
DR EnsemblFungi; YJR130C_mRNA; YJR130C; YJR130C.
DR GeneID; 853594; -.
DR KEGG; sce:YJR130C; -.
DR SGD; S000003891; STR2.
DR VEuPathDB; FungiDB:YJR130C; -.
DR eggNOG; KOG0053; Eukaryota.
DR GeneTree; ENSGT00940000176383; -.
DR HOGENOM; CLU_011302_1_0_1; -.
DR InParanoid; P47164; -.
DR OMA; DVYLFPS; -.
DR BioCyc; MetaCyc:YJR130C-MON; -.
DR BioCyc; YEAST:YJR130C-MON; -.
DR UniPathway; UPA00051; UER00077.
DR PRO; PR:P47164; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47164; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IMP:SGD.
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; IMP:SGD.
DR GO; GO:0019346; P:transsulfuration; IMP:SGD.
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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis; Nucleus;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..639
FT /note="Cystathionine gamma-synthase"
FT /id="PRO_0000114781"
FT MOD_RES 443
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P32929"
SQ SEQUENCE 639 AA; 72351 MW; E94FC84295B538A3 CRC64;
MISRTIGESI PPNTKHAVSV CLPTWEATVG YEEGESSIIN SLTTGYPRFF IHKSIKKLCE
ILSAKYSMED EACLCFPSYK VANRCREFIK VKTGLSTKVR ILQLCTPKPM NQEEKLWRRE
CKITVVFVDQ EIFPVMKQYW QHSGEIVSSR MAEYILHELQ VKDNLKKMET VDNGKKFMTE
DENRVNEEYI ETRFGRNLNF LAADKAKYLI RKRIATKVVE KIDSEGLSDL FSFEHYNESN
GPFNVGSGEA LDDDQLNSDI PAETITSMGE SGSNSTFENT ATDDLKFHVN PNTDVYLFPS
GMASIFTAHR LLLNFDAKRL SRSSSRQDKL IGYGPPFKKT VMFGFPYTDT LSILRKFNHT
HFLGQGDSTS MNALKNILHS GEQILAVFIE APSNPLLKMG DLQELKRLSD LYSFYIVVDE
TVGGFVNIDV LPYADIVCSS LTKIFSGDSN VIAGSLVLNP RGKIYEFARK FMKTEDGYED
CLWCEDALCL ERNSRDFVER TIKVNTNTDI LLKRVLLPQV GKLFKKIYYP SLTSEDTKRN
YDSVMSTKDG GYGGLFSLTF FNIEEAKKFF NNLELCKGPS LGTNFTLACP YAIIAHYQEL
DEVAQYGVET NLVRVSVGLE NSDVLCNVFQ RAIEKALGE
