ID   METXA_LEPME             Reviewed;         379 AA.
AC   P94891;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
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};
OS   Leptospira meyeri.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=29508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serovar Semaranga / isolate Veldrat S 173;
RX   PubMed=9209059; DOI=10.1128/jb.179.13.4396-4398.1997;
RA   Bourhy P., Martel A., Margarita D., Saint Girons I., Belfaiza J.;
RT   "Homoserine O-acetyltransferase, involved in the Leptospira meyeri
RT   methionine biosynthetic pathway, is not feedback inhibited.";
RL   J. Bacteriol. 179:4396-4398(1997).
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; Y10744; CAA71733.1; -; Genomic_DNA.
DR   PIR; T44656; T44656.
DR   AlphaFoldDB; P94891; -.
DR   SMR; P94891; -.
DR   STRING; 1193051.LEP1GSC017_3347; -.
DR   ESTHER; lepme-metx; Homoserine_transacetylase.
DR   BioCyc; MetaCyc:MON-9364; -.
DR   BRENDA; 2.3.1.31; 2987.
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..379
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000155723"
FT   DOMAIN          54..332
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        159
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   379 AA;  41928 MW;  1B891633EDF98ACF CRC64;
     MPTSEQNEFS HGSVGVVYTQ SIRFESLTLE GGETITPLEI AYETYGTLNE KKDNAILVCH
     ALSGDAHAAG FHEGDKRPGW WDYYIGPGKS FDTNRYFIIS SNVIGGCKGS SGPLTINGKN
     GKPFQSTFPF VSIGDMVNAQ EKLISHFGIH KLFAVAGGSM GGMQALQWSV AYPDRLKNCI
     VMASSSEHSA QQIAFNEVGR QAILSDPNWN QGLYTQENRP SKGLALARMM GHITYLSDEM
     MREKFGRKPP KGNIQSTDFA VGSYLIYQGE SFVDRFDANS YIYVTKALDH FSLGTGKELT
     KVLAKVRCRF LVVAYTSDWL YPPYQSEEIV KSLEVNAVPV SFVELNNPAG RHDSFLLPSE
     QQDSILRDFL SSTDEGVFL