ID   METAA_CAMJE             Reviewed;         293 AA.
AC   Q9PLV2; Q0P7Q5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
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}; Synonyms=metA;
GN   OrderedLocusNames=Cj1726c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35820.1; -; Genomic_DNA.
DR   PIR; B81271; B81271.
DR   RefSeq; WP_002783526.1; NC_002163.1.
DR   RefSeq; YP_002345092.1; NC_002163.1.
DR   AlphaFoldDB; Q9PLV2; -.
DR   SMR; Q9PLV2; -.
DR   IntAct; Q9PLV2; 32.
DR   STRING; 192222.Cj1726c; -.
DR   PaxDb; Q9PLV2; -.
DR   PRIDE; Q9PLV2; -.
DR   EnsemblBacteria; CAL35820; CAL35820; Cj1726c.
DR   GeneID; 906001; -.
DR   KEGG; cje:Cj1726c; -.
DR   PATRIC; fig|192222.6.peg.1699; -.
DR   eggNOG; COG1897; Bacteria.
DR   HOGENOM; CLU_057851_0_1_7; -.
DR   OMA; WLWFCYQ; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000000799; 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; Reference proteome; Transferase.
FT   CHAIN           1..293
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_0000199745"
FT   ACT_SITE        141
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        234
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            110
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            190
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ   SEQUENCE   293 AA;  34194 MW;  A843A78723DBD5C2 CRC64;
     MPLIIPENIP AYELLKEHAF IMGLRRAKHQ DIRPQEILIV NLMPKKIETE NQILSLLANS
     PLQVNITLLA TTSYVGKNTP FTHLEKFYKG LEEVKKHKFD GAIVTGAPVE QMDFEKVAYW
     EELLEIFDFL KQNVTSSMYI CWGAMAALKY FYGVDKISLD KKIFGVYKHD KVSPDLLLTN
     LDEKVLMPHS RHSSMDEEQI LALQKQGKLK ILLRNKKIGS ALLRDEKNIF ILGHLEYFKE
     TLHQEYVRDN FIQKAKNYYD KKGNIKYNWR SNANTIFANW LNYDVYQSTP FVL