ID I0IH90_PHYMF Unreviewed; 592 AA.
AC I0IH90;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:BAM04628.1};
GN Synonyms=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
GN OrderedLocusNames=PSMK_24690 {ECO:0000313|EMBL:BAM04628.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM04628.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM04628.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) 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; AP012338; BAM04628.1; -; Genomic_DNA.
DR RefSeq; WP_014437841.1; NC_017080.1.
DR AlphaFoldDB; I0IH90; -.
DR STRING; 1142394.PSMK_24690; -.
DR GeneID; 80848692; -.
DR KEGG; phm:PSMK_24690; -.
DR PATRIC; fig|1142394.8.peg.2549; -.
DR eggNOG; COG2021; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_028760_6_0_0; -.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000007881; Chromosome.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.1740.110; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 InterPro; IPR010743; Methionine_synth_MetW.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 Pfam; PF07021; MetW; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296,
KW ECO:0000313|EMBL:BAM04628.1};
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:UP000007881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 57..366
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 ACT_SITE 327
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT ACT_SITE 360
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 592 AA; 64606 MW; 2541C3BF9DF61805 CRC64;
MGADLPTSSD DLRGAEASSH RRLWRSEEPL SLALGGELPV LEVAYETWGE LAPDGSNAVL
VCHALTGDSH AARHGDDDAA GWWDGLIGPG SAYGIDTTRW YVVCSNVLGG CRGTTGPASV
DPRTGRVYGP DFPVVTIADM VEAQRRLLDG LGVGKLRAVV GGSLGGHQAM TWAITHPGRV
ERCVGIATSP RMSAQALAFD VVARNAIQSD PAFASGRYEA GGGPENGLAI ARMVGHITYL
SPESMDAKFD PDRHEPRDIR TAFEKKFSVG SYLAHQGQKF TQRFDANSYA AITVAMDLFD
LGRTEAERRA KLEPATCHWL FASFSTDWLF RPAQSRQIVD TLTRLGRPVT YTEITSDAGH
DGFLLDAEIA VYGPLVNAFL REPRAEGVEP LRDADRRLLE MIPRDASVLD LGCGDGRLLL
ELGRRNPDRT LAGVEVGQRL LFEAVEHGVD VVDHDLNLGL PGYADGQYDV VVLNVTLQAV
RNTRQLLAEM TRVGRRVLLS FANFAFRELR DDFLRNGRSP LSKSGGGAYD HHWADTPNRR
FPSIRDVEEL LAEMGIRVHR ALYLDTTRGV DVAATDDPNL NADTAILEIS RR
//
