ID   MET2_ASCIM              Reviewed;         518 AA.
AC   P12917;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Homoserine O-acetyltransferase;
DE            EC=2.3.1.31;
DE   AltName: Full=Homoserine O-trans-acetylase;
GN   Name=MET2;
OS   Ascobolus immersus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascobolaceae; Ascobolus.
OX   NCBI_TaxID=5191;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2838393; DOI=10.1016/0378-1119(88)90533-1;
RA   Goyon C., Faugeron G., Rossignol J.-L.;
RT   "Molecular cloning and characterization of the met2 gene from Ascobolus
RT   immersus.";
RL   Gene 63:297-308(1988).
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; M26662; AAA32681.1; -; Genomic_DNA.
DR   PIR; JT0271; XYIMHA.
DR   AlphaFoldDB; P12917; -.
DR   SMR; P12917; -.
DR   ESTHER; ascim-met2; Homoserine_transacetylase.
DR   PRIDE; P12917; -.
DR   UniPathway; UPA00051; UER00074.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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; 2.
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   Transferase.
FT   CHAIN           1..518
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000155754"
FT   DOMAIN          69..468
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          267..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        464
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   518 AA;  57718 MW;  DE17E17B0636E3AC CRC64;
     MHLVDRVGAN APHKKYERVT TQPENPFFNI VHNQSVAIIP SFTLESGVIL YDCPVAYKTF
     GVLNESADNV MVICHALTGS ADVEDWWGPL IGPGRAFDTS RYFIVCCNSM GSPYGSASPC
     TLDSTTGRRY GPEFPLTTVR DDVRYGSTIT MKLGCLLTYY RIHKLIMDDL GVRQIAVVIG
     GSMGGMLALE WAYFGKDYVK AVVALATSAR HSAWCISWGE AQRQSIYSDP KYDDGYYSFS
     DPPYTGLGAA RMSALLTYRS RNSFESRFGR NIPDPSRHPY INTSQPPSHP AEEHYDIHNE
     GFRNRKGFRR SSTTTSDAPP SPTRTSSTSS TDAITPASTT PLHPSRAQPS GIATPPNSVS
     DPFRPVKRPC PTYFSAQSYL RYQADKFVKR FDANCYIAIT RKLDTHDVSR GRTSTLHEAL
     AMIEQPTLII GIESDGLFTF AEQMELAEYI PDARLKRIDS PEGHDAFLIM FAEVNRYICE
     FLREVQPEIM GKEGVHVESK VGEIRASTTG EVEDITHW