ID   METXA_RHOPA             Reviewed;         400 AA.
AC   Q6N1G8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=RPA4437;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572607; CAE29878.1; -; Genomic_DNA.
DR   RefSeq; WP_011159971.1; NC_005296.1.
DR   AlphaFoldDB; Q6N1G8; -.
DR   SMR; Q6N1G8; -.
DR   STRING; 258594.RPA4437; -.
DR   ESTHER; rhopa-metx; Homoserine_transacetylase.
DR   PRIDE; Q6N1G8; -.
DR   EnsemblBacteria; CAE29878; CAE29878; RPA4437.
DR   GeneID; 66895578; -.
DR   KEGG; rpa:RPA4437; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_5; -.
DR   OMA; TRFCVVS; -.
DR   PhylomeDB; Q6N1G8; -.
DR   BioCyc; RPAL258594:TX73_RS22665-MON; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000001426; 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..400
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000155742"
FT   DOMAIN          64..374
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        368
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   400 AA;  43777 MW;  7BAAA1DF9275271B CRC64;
     MMNIHSVKGQ KIAAGERTQE VDHPHSLVAQ FGADQPLPLD CGIELSPFQI AYQTYGTLNA
     DKSNAILVCH ALTMDQHIAN VHPITGKPGG WLTLVGPGKP IDTDRYFVIC SNVIGGCMGS
     TGPASINPAT GKAWGLDFPV ITIPDMVRAQ AMLIDRFGID KLFCVVGGSM GGMQVLQWSV
     AFPERVFSAL AIACATRHSA QNIAFHELGR QAVMADPDWQ HGRYFEHGCF PHRGLAVARM
     AAHITYLSDA ALHRKFGRKM QDRELPTFSF DADFQVESYL RYQGSSFVER FDANSYLYLT
     RAMDYFDIAA DHDGVLAAAF RGTQTRFCVV SFTSDWLFPT SESRAIVHAL NAGGARVSFA
     EIVTDKGHDA FLLDEPEFID IARAFLQSAG TARGLGKAEH