ID A0A235B8F7_9BACL Unreviewed; 367 AA.
AC A0A235B8F7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=CHM34_05605 {ECO:0000313|EMBL:OYD08598.1};
OS Paludifilum halophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Paludifilum.
OX NCBI_TaxID=1642702 {ECO:0000313|EMBL:OYD08598.1, ECO:0000313|Proteomes:UP000215459};
RN [1] {ECO:0000313|EMBL:OYD08598.1, ECO:0000313|Proteomes:UP000215459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102817 {ECO:0000313|EMBL:OYD08598.1,
RC ECO:0000313|Proteomes:UP000215459};
RA Belbahri L.;
RT "The genome sequence of Paludifilum halophilum highlights mechanisms for
RT microbial adaptation to high salt environemnts.";
RL Submitted (JUL-2017) 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:OYD08598.1}.
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DR EMBL; NOWF01000003; OYD08598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235B8F7; -.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000215459; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000215459};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 45..349
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 311
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 344
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 367 AA; 40379 MW; BF933A716008ACCF CRC64;
MPLTVRTSQK QVVPIGSYTP ESGQRIETVE VAVETVGTLT PEKDNAVLVC HALTGDSHAV
GKEGDSGWWD GLIGPGGYID TNRYFVITMN VLGGCDGTTG PSSVNPATGQ PYGSQFPFIT
IRDMVHVQRL CLDRLGVSSL HAVIGGSMGG MMVLEWGVLY PDRVGKLIPI ATAAALSPTA
IAYNDVGRQA ILSDPDFCEG DYYPGPGPVK GLSIARMMGM ITYRTAELFE KRFSRNLQDY
GGSQRSSESV FQIESYLRYQ GRKLVNRFDA NTYLRLLKAM DTHDIGRGRG GKEKALRLIQ
SPVLVIGIRE DMLFPIQQQR ELHDGLFRMN KSSRLVEISS EYGHDAFLVD FKQTGREIES
FLSKDLL
//
