MET2_YEAST
ID MET2_YEAST Reviewed; 486 AA.
AC P08465; D6W0R8;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Homoserine O-acetyltransferase;
DE EC=2.3.1.31;
DE AltName: Full=Homoserine O-trans-acetylase;
GN Name=MET2; OrderedLocusNames=YNL277W; ORFNames=N0615;
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].
RX PubMed=3552887; DOI=10.1016/0378-1119(86)90364-1;
RA Langin T., Faugeron G., Goyon C., Nicolas A., Rossignol J.-L.;
RT "The MET2 gene of Saccharomyces cerevisiae: molecular cloning and
RT nucleotide sequence.";
RL Gene 49:283-293(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hell R.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [6]
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 [7]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine;
CC Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31;
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
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DR EMBL; M15675; AAA34775.1; -; Genomic_DNA.
DR EMBL; AJ001940; CAA05109.1; -; Genomic_DNA.
DR EMBL; Z71553; CAA96188.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10284.1; -; Genomic_DNA.
DR PIR; S63251; S63251.
DR RefSeq; NP_014122.1; NM_001183115.1.
DR AlphaFoldDB; P08465; -.
DR SMR; P08465; -.
DR BioGRID; 35564; 35.
DR DIP; DIP-3985N; -.
DR IntAct; P08465; 2.
DR STRING; 4932.YNL277W; -.
DR ESTHER; yeast-met2; Homoserine_transacetylase.
DR MEROPS; S33.A41; -.
DR iPTMnet; P08465; -.
DR MaxQB; P08465; -.
DR PaxDb; P08465; -.
DR PRIDE; P08465; -.
DR DNASU; 855444; -.
DR EnsemblFungi; YNL277W_mRNA; YNL277W; YNL277W.
DR GeneID; 855444; -.
DR KEGG; sce:YNL277W; -.
DR SGD; S000005221; MET2.
DR VEuPathDB; FungiDB:YNL277W; -.
DR eggNOG; ENOG502QRIX; Eukaryota.
DR HOGENOM; CLU_028760_5_0_1; -.
DR InParanoid; P08465; -.
DR OMA; TRFCVVS; -.
DR BioCyc; MetaCyc:YNL277W-MON; -.
DR BioCyc; YEAST:YNL277W-MON; -.
DR SABIO-RK; P08465; -.
DR UniPathway; UPA00051; UER00074.
DR PRO; PR:P08465; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P08465; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IDA:SGD.
DR GO; GO:0009092; P:homoserine metabolic process; IDA:SGD.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:SGD.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..486
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155758"
FT DOMAIN 66..436
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 248..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 401
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 430
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT CONFLICT 429..486
FT /note="GHDAFLLEFKLINKLIVQFLKTNCKAITDAAPRAWGGDVGNDETKTSVFGEA
FT EEVTNW -> ATMPSYWSLS (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53659 MW; FD5E8B9D0CE8C707 CRC64;
MSHTLKSKTL QELDIEEIKE TNPLLKLVQG QRIVQVPELV LESGVVINNF PIAYKTWGTL
NEAGDNVLVI CHALTGSADV ADWWGPLLGN DLAFDPSRFF IICLNSMGSP YGSFSPLTIN
EETGVRYGPE FPLCTVRDDV RAHRIVLDSL GVKSIACVIG GSMGGMLSLE WAAMYGKEYV
KNMVALATSA RHSAWCISWS EAQRQSIYSD PNYLDGYYPV EEQPVAGLSA ARMSALLTYR
TRNSFENKFS RRSPSIAQQQ KAQREETRKP STVSEHSLQI HNDGYKTKAS TAIAGISGQK
GQSVVSTASS SDSLNSSTSM TSVSSVTGEV KDIKPAQTYF SAQSYLRYQG TKFINRFDAN
CYIAITRKLD THDLARDRVD DITEVLSTIQ QPSLIIGIQS DGLFTYSEQE FLAEHIPKSQ
LEKIESPEGH DAFLLEFKLI NKLIVQFLKT NCKAITDAAP RAWGGDVGND ETKTSVFGEA
EEVTNW
