ID   METXA_RHOPB             Reviewed;         400 AA.
AC   Q20YI1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=RPC_4281;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-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; CP000301; ABD89805.1; -; Genomic_DNA.
DR   RefSeq; WP_011474686.1; NC_007925.1.
DR   AlphaFoldDB; Q20YI1; -.
DR   SMR; Q20YI1; -.
DR   STRING; 316056.RPC_4281; -.
DR   ESTHER; rhopb-q20yi1; Homoserine_transacetylase.
DR   EnsemblBacteria; ABD89805; ABD89805; RPC_4281.
DR   KEGG; rpc:RPC_4281; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_5; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00074.
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; Transferase.
FT   CHAIN           1..400
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_1000021902"
FT   DOMAIN          64..373
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  43976 MW;  FD50745D1DF5B6F6 CRC64;
     MVKVQSIQSQ AVHAEERAHE ADHPSSQVAL FGADQPLRLD CGVDLAPFQI AYQTYGALNA
     DKSNAILVCH ALTGDQHVAN IHPVTGKPGW WQTLVGPGKP LDPERFFIIC SNVIGSCMGS
     TGPSSTNPLT GKPWGLDFPI ITIPDMVRAQ AMLIDRLGID RLFCVVGGSM GGMQTLQWSV
     AYPKRVASAL AIACSTRHSA QNIAFHELGR QAVMADPEWH HGRYYEEGSY PHRGLGVARM
     AAHITYLSDA ALHRKFGRRM QDRELPTFSF DADFQVESYL RYQGSSFVER FDANSYLYLT
     RAMDYFDIAA DHDGVLAEAF RDTTTRFCVV SFTSDWLFPT SESRNVVHAL NAGGARVSFA
     EIETDRGHDA FLLDVPEFVD IVRAFLQSAG VAHGLAGKGH