ID   MET2_EMENI              Reviewed;         489 AA.
AC   Q9Y875; C8VMS1; Q5BB51;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Homoserine O-acetyltransferase;
DE            EC=2.3.1.31;
DE   AltName: Full=Homoserine O-trans-acetylase;
GN   Name=metE; ORFNames=AN2229;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11406274; DOI=10.1016/s0167-4781(01)00224-x;
RA   Grynberg M., Piotrowska M., Pizzinini E., Turner G., Paszewski A.;
RT   "The Aspergillus nidulans metE gene is regulated by a second system
RT   independent from sulphur metabolite repression.";
RL   Biochim. Biophys. Acta 1519:78-84(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC       {ECO:0000305}.
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DR   EMBL; AF162658; AAD43584.1; -; Genomic_DNA.
DR   EMBL; AACD01000036; EAA63914.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF86426.1; -; Genomic_DNA.
DR   RefSeq; XP_659833.1; XM_654741.1.
DR   AlphaFoldDB; Q9Y875; -.
DR   SMR; Q9Y875; -.
DR   STRING; 162425.CADANIAP00008915; -.
DR   ESTHER; emeni-met2; Homoserine_transacetylase.
DR   PRIDE; Q9Y875; -.
DR   EnsemblFungi; CBF86426; CBF86426; ANIA_02229.
DR   EnsemblFungi; EAA63914; EAA63914; AN2229.2.
DR   GeneID; 2874619; -.
DR   KEGG; ani:AN2229.2; -.
DR   VEuPathDB; FungiDB:AN2229; -.
DR   eggNOG; ENOG502QRIX; Eukaryota.
DR   HOGENOM; CLU_028760_5_0_1; -.
DR   InParanoid; Q9Y875; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 1090515at2759; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006555; P:methionine metabolic process; IEP:AspGD.
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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Methionine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..489
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000155755"
FT   DOMAIN          63..435
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          247..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   489 AA;  53992 MW;  D7427932B7BADAE4 CRC64;
     MTTEQPTARL QRVDSQPENP FSALIEDQSI VIIPTFTLES GVTLYNVPVA YTTRGTLSPS
     GDNALVICHA LSGSADVADW WGPLLGGPGQ AFDISRFFVV CLNSLGSPYG SASAVTYKDG
     NPEKGLYGPE FPLTTVRDDV RIHKMVLDDL GIKQIAAVVG GSMGGMLTLE YAYFGKDYVR
     AIVPIATSAR HSAWCISWGE AQRQSIYSDP KYENGYYSFD EPPAAGLGAA RMSALLTYRS
     RNSFESRFGR NVPDPSKRQN INGTERLPTP PNEHWAIHND GHKGNWSGRN SPAPEKPAEK
     TEVQYMDPQF SGTKTFSKSV STTDGNAQKR PATYFSAQSY LRYQGDKFVK RFDANCYIAI
     TRKLDTHDVS RHRARPDSEN PVREALSQIQ QPALVLGIES DGLFTFEEQK EIAEGIPDSR
     LKRIDSPEGH DAFLLQFEQV NQYILEFFRE VLPDIMSKTP TDGAAIDGVG KLTKSSTFGE
     AEVEDITAW