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   27-MAR-2024, entry version 186.
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; 36.
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; 4932-YNL277W; -.
DR   PeptideAtlas; P08465; -.
DR   DNASU; 855444; -.
DR   EnsemblFungi; YNL277W_mRNA; YNL277W; YNL277W.
DR   GeneID; 855444; -.
DR   KEGG; sce:YNL277W; -.
DR   AGR; SGD:S000005221; -.
DR   SGD; S000005221; MET2.
DR   VEuPathDB; FungiDB:YNL277W; -.
DR   eggNOG; ENOG502QRIX; Eukaryota.
DR   HOGENOM; CLU_028760_5_0_1; -.
DR   InParanoid; P08465; -.
DR   OMA; SYLHYQG; -.
DR   OrthoDB; 2600616at2759; -.
DR   BioCyc; MetaCyc:YNL277W-MONOMER; -.
DR   BioCyc; YEAST:YNL277W-MONOMER; -.
DR   SABIO-RK; P08465; -.
DR   UniPathway; UPA00051; UER00074.
DR   BioGRID-ORCS; 855444; 0 hits in 10 CRISPR screens.
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; alpha/beta hydrolase; 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   NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR   PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//