ID   METXA_DEIRA             Reviewed;         334 AA.
AC   Q9RVZ8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=DR_0872;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF10449.1; -; Genomic_DNA.
DR   PIR; F75463; F75463.
DR   RefSeq; NP_294596.1; NC_001263.1.
DR   RefSeq; WP_010887517.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RVZ8; -.
DR   SMR; Q9RVZ8; -.
DR   STRING; 243230.DR_0872; -.
DR   ESTHER; deira-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; AAF10449; AAF10449; DR_0872.
DR   KEGG; dra:DR_0872; -.
DR   PATRIC; fig|243230.17.peg.1057; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_0; -.
DR   InParanoid; Q9RVZ8; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..334
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000155716"
FT   DOMAIN          61..318
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        148
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   334 AA;  35406 MW;  E44CE45580D22725 CRC64;
     MTAVLAGHAS ALLLTEEPDC SGPQTVVLFR REPLLLDCGR ALSDVRVAFH TYGTPRADAT
     LVLHALTGDS AVHEWWPDFL GAGRPLDPAD DYVVCANVLG GCAGTTSAAE LAATCSGPVP
     LSLRDMARVG RALLDSLGVR RVRVIGASMG GMLAYAWLLE CPDLVEKAVI IGAPARHSPW
     AIGLNTAARS AIALAPGGEG LKVARQIAML SYRSPESLSR TQAGQRVPGV PAVTSYLHYQ
     GEKLAARFDE QTYCALTWAM DAFQPSSADL KAVRAPVLVV GISSDLLYPA AEVRACAAEL
     PHADYWELGS IHGHDAFLMD PQDLPERVGA FLRS