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Database: UniProt
Entry: A0A369QSV4_9BACT
LinkDB: A0A369QSV4_9BACT
Original site: A0A369QSV4_9BACT 
ID   A0A369QSV4_9BACT        Unreviewed;       506 AA.
AC   A0A369QSV4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=metX {ECO:0000313|EMBL:RDC65248.1};
GN   Synonyms=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
GN   ORFNames=AHMF7616_03878 {ECO:0000313|EMBL:RDC65248.1};
OS   Adhaeribacter pallidiroseus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=2072847 {ECO:0000313|EMBL:RDC65248.1, ECO:0000313|Proteomes:UP000253919};
RN   [1] {ECO:0000313|EMBL:RDC65248.1, ECO:0000313|Proteomes:UP000253919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7616 {ECO:0000313|EMBL:RDC65248.1,
RC   ECO:0000313|Proteomes:UP000253919};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Adhaeribacter sp. HMF7616 genome sequencing and assembly.";
RL   Submitted (APR-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDC65248.1}.
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DR   EMBL; QASA01000001; RDC65248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369QSV4; -.
DR   OrthoDB; 9800754at2; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000253919; Unassembled WGS sequence.
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; 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   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296,
KW   ECO:0000313|EMBL:RDC65248.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000253919};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00296}.
FT   DOMAIN          40..322
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   506 AA;  57475 MW;  E571A019EDFA8EC7 CRC64;
     MSQEILHYPQ PFLLECGKTL PQLQITYHTY GTYNPEKNNV IWVCHALTAN ADVFDWWKGL
     FGSGCLFNPD DYFIVCANIL GSCYGTTGPL AENIATGAAY FQLFPDISIR DMVAAHEILR
     QHLGIFKIYS LIGGSLGGQQ ALEWSIQYPD LIENLLIVAT NASHSPWGIA FNEAQRMAIR
     ADETYNLNVP EGGRKGLKAA RAVALLSYRT YHTYGRTQCE TDLNKTDNFK ASSYQNYQGD
     KLVNRFNAYS YVSLSKTMDS HNVGRNQPSI EQALQQIKAK TLVIGISSDL LFPPQEQQYL
     TEHIPGAVYH EIDSFYGHDG FLIETEKLTQ LIETFLAVPI TPQLKLDKMI SQIVKEEFYF
     RGAFMSLFID IEFLLGDTIA TILTGDNELK LNLIEFVNPK LMLEPKLSLL HKILNQKYFD
     LYSKKYKDGI NELRKFTDLR NSFAHKRISI DNGNKKLNFI VMDNGKLIDN SFTFENLETK
     FTELKALLTL VNTLHDEIVK SQTDKA
//
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