ID   METXA_MYCBP             Reviewed;         379 AA.
AC   A1KP32;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BCG_3411;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL73400.1; -; Genomic_DNA.
DR   RefSeq; WP_003417458.1; NC_008769.1.
DR   AlphaFoldDB; A1KP32; -.
DR   SMR; A1KP32; -.
DR   ESTHER; myctu-metx; Homoserine_transacetylase.
DR   KEGG; mbb:BCG_3411; -.
DR   HOGENOM; CLU_028760_1_0_11; -.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000001472; 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:0016787; F:hydrolase activity; IEA:UniProt.
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_1000021884"
FT   DOMAIN          52..356
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   379 AA;  39769 MW;  6F3506E4CC094D43 CRC64;
     MTISDVPTQT LPAEGEIGLI DVGSLQLESG AVIDDVCIAV QRWGKLSPAR DNVVVVLHAL
     TGDSHITGPA GPGHPTPGWW DGVAGPGAPI DTTRWCAVAT NVLGGCRGST GPSSLARDGK
     PWGSRFPLIS IRDQVQADVA ALAALGITEV AAVVGGSMGG ARALEWVVGY PDRVRAGLLL
     AVGARATADQ IGTQTTQIAA IKADPDWQSG DYHETGRAPD AGLRLARRFA HLTYRGEIEL
     DTRFANHNQG NEDPTAGGRY AVQSYLEHQG DKLLSRFDAG SYVILTEALN SHDVGRGRGG
     VSAALRACPV PVVVGGITSD RLYPLRLQQE LADLLPGCAG LRVVESVYGH DGFLVETEAV
     GELIRQTLGL ADREGACRR