ID A0A0J1B8Q6_RHOIS Unreviewed; 603 AA.
AC A0A0J1B8Q6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=RISK_004512 {ECO:0000313|EMBL:KLU03200.1};
OS Rhodopirellula islandica.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=595434 {ECO:0000313|EMBL:KLU03200.1, ECO:0000313|Proteomes:UP000036367};
RN [1] {ECO:0000313|EMBL:KLU03200.1, ECO:0000313|Proteomes:UP000036367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24040 / K833 {ECO:0000313|Proteomes:UP000036367};
RA Kizina J., Richter M., Glockner F.O., Harder J.;
RT "Permanent draft genome of Rhodopirellula islandicus K833.";
RL Submitted (MAY-2015) 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:KLU03200.1}.
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DR EMBL; LECT01000038; KLU03200.1; -; Genomic_DNA.
DR RefSeq; WP_047815761.1; NZ_LECT01000038.1.
DR AlphaFoldDB; A0A0J1B8Q6; -.
DR STRING; 595434.RISK_004512; -.
DR PATRIC; fig|595434.4.peg.4285; -.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000036367; 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 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 NCBIfam; TIGR02081; metW; 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:KLU03200.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 61..368
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT ACT_SITE 331
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT ACT_SITE 364
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 603 AA; 66885 MW; 63EE919561886EF4 CRC64;
MGELSNEDLS STDDVRTDAP LTHAKYVTFD QPLTLERGGE LPEVRCCFET WGRLNAEASN
AILVCHAVSG DSHAARHNQD DEPGWWDGLI GPGLPLDTDR FFVVCPNVLG GCRGSTGPGD
ADPTSPDGKP YGANFPRITI GDIVEVQKRL ADHLGIQQWR AVVGGSLGGH QVLQWINRYP
DAAKTCIAIA TSPRLNSQAL GFDVIARNAI QTDPHYADGQ YYNQAQRPDT GLAIARMLGH
ITYLSVEAME AKFDPDRHDP RQIASQFEQR FSIGSYLAHQ GQKFTTRFDA NSYVTLSMAM
DLFDLGGTRL KLMETFDEAS CDFLLISFSS DWLFPPAQSR EVVNALTALD KRVTYAEITT
NAGHDAFLIA KDIATYGPLV RERLRDPETR PEVPSETRLS VDEESILEII PTGASVLDLG
CGNGQLLAAI RDRHVEPGQR LMGVEVAQEN LLSTAMRGID VIDYDLNNGL PAFIDNQFDY
VVLNATLQAV ENVVELLDEM LRVGRHAIIS FPNFAYRQLR DHYVTHGRSP KAPGEFDFDW
HNTPNRRFPT IADVRDLLGQ LNVVIDQEVF WDVDQGQRIE PDNDPNLNAD TAVIAFHRES
QPT
//
