METW_YEAST
ID METW_YEAST Reviewed; 575 AA.
AC Q12198; D6VXV0;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Putative cystathionine gamma-synthase YLL058W;
DE EC=2.5.1.48;
DE AltName: Full=O-succinylhomoserine (thiol)-lyase;
GN OrderedLocusNames=YLL058W; ORFNames=L0569;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Wedler H., Wambutt R.;
RT "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces
RT cerevisiae including the subtelomeric region of the left arm.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [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., 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 (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 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; Z47973; CAA87999.1; -; Genomic_DNA.
DR EMBL; Z73163; CAA97511.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09266.1; -; Genomic_DNA.
DR PIR; S50962; S50962.
DR RefSeq; NP_013042.1; NM_001181878.1.
DR AlphaFoldDB; Q12198; -.
DR SMR; Q12198; -.
DR BioGRID; 31257; 51.
DR STRING; 4932.YLL058W; -.
DR MaxQB; Q12198; -.
DR PaxDb; Q12198; -.
DR PRIDE; Q12198; -.
DR EnsemblFungi; YLL058W_mRNA; YLL058W; YLL058W.
DR GeneID; 850668; -.
DR KEGG; sce:YLL058W; -.
DR SGD; S000003981; YLL058W.
DR VEuPathDB; FungiDB:YLL058W; -.
DR eggNOG; KOG0053; Eukaryota.
DR GeneTree; ENSGT00940000176383; -.
DR HOGENOM; CLU_011302_1_0_1; -.
DR InParanoid; Q12198; -.
DR OMA; LACPYVH; -.
DR BioCyc; YEAST:G3O-32157-MON; -.
DR UniPathway; UPA00051; UER00077.
DR PRO; PR:Q12198; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12198; protein.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; ISS: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; 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; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..575
FT /note="Putative cystathionine gamma-synthase YLL058W"
FT /id="PRO_0000114782"
FT MOD_RES 376
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 575 AA; 64223 MW; EDE6292C60ADFDC1 CRC64;
MTEIEFGQPL PSNLDYAVSF GIPTWDSAIG YAEKVPEVIG KMATGYPRYF PQPPVQRLCA
YFVKKFGRGS ENCRPFPSVN LGLKCFEYVK SVSGPESKAH LEVETVTIKN RGAKTSKEPA
ELVLTIAAVL ASEEEFETVK EYWKLRGECV SSRLALSVNQ LLDCANHGSE QVLRELEAGV
FAAKKGEEKA KNLIKGRIVE NRFRPFGLEK KTPNWEGLNL NPNEDVYLVS SGMSAISTAR
NLLTFWEEKK NSGDSLNKTT SDQKKKPLLC DTVGIFGFPF KDTQVIMTKF GKCKFFGFGN
SRDVVELQKF LETSKQRILA VFVETPSNPL LNMPDLKKLR SLADQYGFFI VIDDTIGGLN
VDILPYADIV STSLTKLFNG ASNVMGGSVV LNPKSSLYPY AREYFRSANF EDLLWCEDAI
VLERNSRDFE DRTLRANANT GILLNDLLLP EEGKICKKIY YPTVTSKETF ENYESVRNER
GGYGCLFSVA FFNEGDAKAF YDSLKVFKGP SNGTNFTLAC PYVHLAHHSE LEEVSKFGAD
PNIIRVSVGL EDIQWLLKVF SSALDVVKSR GSKHS
