ID A0A1H6IVN8_9EURY Unreviewed; 462 AA.
AC A0A1H6IVN8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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};
GN ORFNames=SAMN05192561_103238 {ECO:0000313|EMBL:SEH50530.1};
OS Halopenitus malekzadehii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1267564 {ECO:0000313|EMBL:SEH50530.1, ECO:0000313|Proteomes:UP000199215};
RN [1] {ECO:0000313|EMBL:SEH50530.1, ECO:0000313|Proteomes:UP000199215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10418 {ECO:0000313|EMBL:SEH50530.1,
RC ECO:0000313|Proteomes:UP000199215};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00003082,
CC 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|ARBA:ARBA00001480, ECO:0000256|HAMAP-
CC 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; FNWU01000003; SEH50530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6IVN8; -.
DR STRING; 1267564.SAMN05192561_103238; -.
DR OrthoDB; 295172at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000199215; 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 PIRSF; PIRSF000443; Homoser_Ac_trans; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00296}; 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:UP000199215};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 119..414
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 56..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 374
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 407
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 462 AA; 49162 MW; 6E3E67A4D1BDFEE8 CRC64;
MTTTPHDSGI VPLGEFTFEC GRSIPELRIA YETYGEFTGE NAVLVCHALT GSQNVARTPE
IPDTDASGGA GTGDAVGSDA AADEGVDADA EIDAGADGDP PNQAGQARAW WDDVVGPGKA
IDTTEYYVVC ANVPGSCYGS SGPASRRPDD VDPDREVDHD RWALDFPPVQ VGDWTRAQRR
LLDHLGVGRL HAVVGGSVGG MNVLDWGKRY PDDADHLVAI ATAARLDPQC LALDAIARRA
IRSDPDWNGG DYYGDRPGPD TGLGLARQIG HVMYLSKSSM DRKFGRRSAG RDSLTRGEGL
DVPENPTAAF FPYREVESYL DYNAGSFADR FDANSYLYLT RAMDEYDLAG GYASDADALA
AFTGEALVMS FTDDWHFTVD QSVALADAFG DADVPVAHHI VDSDHGHDAF LVEPESVGPP
VRDFLRSGID GKSIVDAAES DEPVTDGSGT SHAPVHSSLF SG
//
