ID   METXA_SYNC1             Reviewed;         372 AA.
AC   Q3A7G2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE            Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296};
DE            EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296};
DE   AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE            Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296};
GN   Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296}; OrderedLocusNames=Pcar_0422;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC       forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00296};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00296}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC       {ECO:0000255|HAMAP-Rule:MF_00296}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000142; ABA87682.2; -; Genomic_DNA.
DR   RefSeq; WP_011340104.1; NC_007498.2.
DR   AlphaFoldDB; Q3A7G2; -.
DR   SMR; Q3A7G2; -.
DR   STRING; 338963.Pcar_0422; -.
DR   ESTHER; pelcd-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; ABA87682; ABA87682; Pcar_0422.
DR   KEGG; pca:Pcar_0422; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_7; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000002534; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
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; Cytoplasm;
KW   Methionine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..372
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000231878"
FT   DOMAIN          49..356
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        349
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   372 AA;  41794 MW;  343E8A163A3B946C CRC64;
     MEPSVGIVKT RHIDFNGDLR LESGRLLAAP ITLAYETYGQ LNADRSNGIL VTHAWTGDAH
     AAGRHTPEDR KPGWWDDMIG PGKVLDTNRY FVICSNVIGS CGGSTGPTSI NPRTGRPYNL
     SFPVIMVRDM VRAQKRLIDH LDLPSLVTVI GGSMGAMQAL EWGVLFPDTV RSIIPIAGTG
     RTSPMAIALN ALARQAIFND PMWKKGNYRP EHPPADGLAL GRAIGHISFL SNASMHLKFG
     RRFSARDGMF DFFGQFEVER YLEYNGRAFI DRFDTNAFLY LAKALDLYDV AWNYDSREQA
     LDRIQCPSLW FTFSSDWLYP PQEAEDIVNI LQKLGKPAEY HPIQSDYGHD SFLVEPEKFT
     HHITEFLNRL TV