ID   METAA_BRUAB             Reviewed;         306 AA.
AC   Q577P3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=BruAb2_0737;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX76141.1; -; Genomic_DNA.
DR   RefSeq; WP_002966142.1; NC_006933.1.
DR   AlphaFoldDB; Q577P3; -.
DR   SMR; Q577P3; -.
DR   EnsemblBacteria; AAX76141; AAX76141; BruAb2_0737.
DR   GeneID; 45053533; -.
DR   GeneID; 55592168; -.
DR   KEGG; bmb:BruAb2_0737; -.
DR   HOGENOM; CLU_057851_0_1_5; -.
DR   OMA; WLWFCYQ; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000000540; Chromosome II.
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..306
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_1000021804"
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   306 AA;  35245 MW;  E942A97E01C13E47 CRC64;
     MPIKIPDDLP ATSVLEAEGV MVMREADAVR QDIRPLRIGL LNLMPNKVTT ETQIARLLGA
     TPLQVELTLV RMTNHVARHT PADHMLSFYC PWEEVNDQRF DGFVITGAPV ERLPFEEVTY
     WDEMRRVFDW TQSHVHRTLN ICWAAQAAVY HFHGMKKYDL PAKASGVFRQ RSLVPASPYL
     RGFSDDFAIP VSRWTEVRKS DIPADSGLKV LVDSTETGLC LLDDPRHRSL HMFNHVEYDT
     TSLADEYFRD IQVQPEAKVP VNYFPGDDAK RPPENRWRSH AHLLFGNWIN EMYQSTPYDI
     ERIGKV