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Database: UniProt
Entry: E7C5I9_9BACT
LinkDB: E7C5I9_9BACT
Original site: E7C5I9_9BACT 
ID   E7C5I9_9BACT            Unreviewed;       380 AA.
AC   E7C5I9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Homoserine O-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
DE            Short=HAT {ECO:0000256|HAMAP-Rule:MF_00296};
DE            EC=2.3.1.31 {ECO:0000256|HAMAP-Rule:MF_00296};
DE   AltName: Full=Homoserine transacetylase {ECO:0000256|HAMAP-Rule:MF_00296};
DE            Short=HTA {ECO:0000256|HAMAP-Rule:MF_00296};
GN   Name=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
OS   uncultured verrucomicrobium HF0500_27H16.
OC   Bacteria; Verrucomicrobiota; environmental samples.
OX   NCBI_TaxID=723600 {ECO:0000313|EMBL:ADI22713.1};
RN   [1] {ECO:0000313|EMBL:ADI22713.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pham V.D., Delong E.F.;
RT   "Genome fragments of uncultured bacteria from the North Pacific subtropical
RT   Gyre.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC       forming acetyl-L-homoserine. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00296}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC       {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
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DR   EMBL; GU567995; ADI22713.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7C5I9; -.
DR   UniPathway; UPA00051; UER00074.
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; 1.10.1740.110; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR   PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00296}.
FT   DOMAIN          59..362
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   380 AA;  42493 MW;  FB83678EA580BC75 CRC64;
     MPTEQIDASP WKAVDNVGLV QPRDYHHAQS FTFDNGQSIP ELKIRYETYG DLNTDHSNAI
     LVCHALSGDH HCAGYHEGAR KPGWWDNMIG PGKPIDTGRF HVICPNCLGG CQGTTGPASI
     NPESGKPYNQ DFPRITIGDM VRAQKLLLNH MGIQNLYAAV GGSMGGMQVM QWMIDYPEVA
     KRVLILASTA RQSTQAIAFD EVGRSAIHQD PNWNGGDYDP ENGPDTGLAI ARMMAHITYL
     SNRGLESKFG RSRRQEAEKL TEVEFEVESY LRHQGRSFVN RFDANTYLHF TKALDVFDLY
     GEGDDLTQAF KNVQARILAI GFTSDWLYSP EENRDIIQAL LKLGKDASYA ELEAELGHDS
     FLLESEEYFN LVRAFLAEAR
//
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