ID   METAA_ALKCL             Reviewed;         309 AA.
AC   A0A1D3PDD4;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
DE            EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:28581482};
DE   AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HTA {ECO:0000255|HAMAP-Rule:MF_00295};
GN   Name=metAA {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
GN   Synonyms=metA {ECO:0000312|EMBL:SCN13862.1};
OS   Alkalihalobacillus clausii (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=79880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 8716;
RX   PubMed=28581482; DOI=10.1038/nchembio.2397;
RA   Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA   Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA   Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA   Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT   "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT   biosynthesis.";
RL   Nat. Chem. Biol. 13:858-866(2017).
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC       forming acetyl-L-homoserine. In vitro, can also use propionyl-CoA as
CC       acyl donor. {ECO:0000269|PubMed:28581482}.
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_00295,
CC         ECO:0000269|PubMed:28581482};
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_00295}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC   -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00295}.
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DR   EMBL; LT613638; SCN13862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D3PDD4; -.
DR   SMR; A0A1D3PDD4; -.
DR   OMA; WLWFCYQ; -.
DR   UniPathway; UPA00051; UER00074.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro.
DR   CDD; cd03131; GATase1_HTS; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00295; MetA_acyltransf; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005697; HST_MetA.
DR   InterPro; IPR033752; MetA_family.
DR   PANTHER; PTHR20919; PTHR20919; 1.
DR   Pfam; PF04204; HTS; 1.
DR   PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01001; metA; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Transferase.
FT   CHAIN           1..309
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000440336"
FT   ACT_SITE        148
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            117
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            198
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ   SEQUENCE   309 AA;  35773 MW;  AE2F2D7B46CF6DE4 CRC64;
     MRERVAMPIK IPDHLPAKEI LLKENIFIMD ESRAYTQDIR PLKICILNLM PTKQETETQL
     LRLLGNTPLQ VDVSLLHPST HSPRNTSKEH LNLFYKTIDE VKQQKFDGMI ITGAPVETLP
     FHDVNYWNEM TSILDWTTTN VTSTLHICWG AQAGLYHHYG IKKKPLTTKL FGVYSHKLEV
     KNVNLLRGFD DVFYAPHSRH TTVSREDIER VDELIVLSSS EEAGVYIASS KDGKRVFVMG
     HSEYDAHTLK QEYERDVKRG IACDPPFNYF PEGNVDALPP LQWRAHSNLL FSNWLNYYVY
     QETPYHLDD