ID   METXA_PELPD             Reviewed;         371 AA.
AC   A1AUS2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Ppro_3500;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) 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}.
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DR   EMBL; CP000482; ABL01093.1; -; Genomic_DNA.
DR   RefSeq; WP_011737308.1; NC_008609.1.
DR   AlphaFoldDB; A1AUS2; -.
DR   SMR; A1AUS2; -.
DR   STRING; 338966.Ppro_3500; -.
DR   ESTHER; pelpd-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; ABL01093; ABL01093; Ppro_3500.
DR   KEGG; ppd:Ppro_3500; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_7; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000006732; 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..371
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_1000021892"
FT   DOMAIN          44..350
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   371 AA;  41259 MW;  860B944F14182932 CRC64;
     MSVSIVREQS ITISDGIRLD SGRILAPITI AYETYGTLNT DASNAILVEH AWTGSAHLAG
     KQSENDTKPG WWDAIVGPGR LLDTDRYFVI CSNVIGSCFG STGPASINPK TGKRYNLTFP
     VITIRDMVRA QKLLIEMLGI RRLLSVMGGS MGGMQTLEWI TQYPDAIASA VLLATTPRPS
     PLAISMNAIA RWSIFNDPTW RKGEYKNNPK DGLALARAIG HITFLSDESM QAKFGRKFSA
     RDGQFDFFGQ FEVERYLDYN GYSFVSRFDA NSFLYLAKAL DLYDVSWGYE SMAEAFARVS
     APLQFFAFSS DWLYPPGQTE EMVSCLRKLG KEVEYHLISS SYGHDAFLLE HEAFSPLVKR
     FLDAAYAKGG Q