ID   METXA_GRABC             Reviewed;         406 AA.
AC   Q0BVW2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=GbCGDNIH1_0142;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(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; CP000394; ABI61040.1; -; Genomic_DNA.
DR   RefSeq; WP_011630850.1; NC_008343.2.
DR   AlphaFoldDB; Q0BVW2; -.
DR   SMR; Q0BVW2; -.
DR   STRING; 391165.GbCGDNIH1_0142; -.
DR   ESTHER; grabc-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; ABI61040; ABI61040; GbCGDNIH1_0142.
DR   KEGG; gbe:GbCGDNIH1_0142; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_0_5; -.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000001963; 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: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; Reference proteome; Transferase.
FT   CHAIN           1..406
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_1000021878"
FT   DOMAIN          47..368
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        329
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   406 AA;  43823 MW;  7C56AEB71FA2B93E CRC64;
     MKRSVNTAPQ KDVFVFRDGL PLDNGGSLDG IRIAYRTYGA LNAEASNAIL VCHALTGDQY
     VADPNPVTGK PGWWYGVVGP GCPIDTNRYF VICSNVIGGC MGSTGPRSPR DPALPDDAAG
     VELWGTDFPS LTIRDMVRAQ KKLIEHLGIA RLFAVIGGSF GGMQALQWAA SYPDAVFAAI
     PIATASFHSA QNIAFNEVGR QAIFGDPNWN GGGYWRTGHM PERGLAVARM VAHITYLSEQ
     ALARKFGRRV RRDGMGGETA ANLFGEMFEV ESYLRYQGGA FVKRFDANSY LTITRAADHF
     DLAEEYGGDL AAAFAGTKTR FCVISFSSDW LYPTAESRHI ARALNRVAAN VSFVEVTSDK
     GHDAFLLDEP DFHRVLNGFL EGCADHAGLA FNGFGGGSAL LRVEAS