ID   METAA_DESHD             Reviewed;         307 AA.
AC   B8FWT4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295};
DE            EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295};
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}; OrderedLocusNames=Dhaf_4581;
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2;
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC       forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00295}.
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   -!- 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; CP001336; ACL22582.1; -; Genomic_DNA.
DR   RefSeq; WP_015945319.1; NC_011830.1.
DR   AlphaFoldDB; B8FWT4; -.
DR   SMR; B8FWT4; -.
DR   PRIDE; B8FWT4; -.
DR   EnsemblBacteria; ACL22582; ACL22582; Dhaf_4581.
DR   KEGG; dhd:Dhaf_4581; -.
DR   HOGENOM; CLU_057851_0_1_9; -.
DR   OMA; WLWFCYQ; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000007726; Chromosome.
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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Transferase.
FT   CHAIN           1..307
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_1000191182"
FT   ACT_SITE        142
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            111
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            192
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ   SEQUENCE   307 AA;  35840 MW;  69625C46B1A0719E CRC64;
     MPINVPDGLP AAEILTKEDV FIMEEKRAEH QDIRPLSIVI LNLMPNKIIT ETQILRLLGN
     SPLQVDITLL YPETHRSKNT PEEYLIKYYQ TFDSIKDQKF DGMIITGAPI EQMPFEEVDF
     WPELQKIMDW SKANVFSTLF ICWGAQAGLY HFFGVPKYPL PAKMFGVFPH TLNRRDIRLL
     RGFDDIFYVP HSRHTEVRKE DIVKVPELEI LSESEESGVY LVGTKGGRQI FVTGHSEYDP
     YTLKAEYDRD ISYELPINVP QNYYPGDDPR QTPVVRWRGH SNLLFANWLN YYVYQETPYN
     LEELGNR