ID D5UIM2_CELFN Unreviewed; 436 AA.
AC D5UIM2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Cfla_0609 {ECO:0000313|EMBL:ADG73521.1};
OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG73521.1, ECO:0000313|Proteomes:UP000000849};
RN [1] {ECO:0000313|EMBL:ADG73521.1, ECO:0000313|Proteomes:UP000000849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX PubMed=21304688; DOI=10.4056/sigs.1012662;
RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL Stand. Genomic Sci. 3:15-25(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001964; ADG73521.1; -; Genomic_DNA.
DR RefSeq; WP_013115855.1; NC_014151.1.
DR AlphaFoldDB; D5UIM2; -.
DR STRING; 446466.Cfla_0609; -.
DR KEGG; cfl:Cfla_0609; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_0_11; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000849; 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 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 ECO:0000313|EMBL:ADG73521.1};
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:UP000000849};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 111..415
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 381
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 411
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 436 AA; 46370 MW; C56AFCF12EA2CC62 CRC64;
MTQPDPRTDA PDRTPDRRAM PGAYPGAGSG DVGVPDPLVG RRARRGATLG SRVPPAQRPP
VPATAAWRDG DDPGRRQFAD LGPLKLESGG RLPTVRLAYE TWGELDEDGS NAVLVLHALT
GDSHVTGDAG PGHPTPGWWQ SMVGPGAPID TDRWFVVAPN ALGGCQGSTG PASTAPDGRP
WGGRFPLLTV RDQVAAEVRL ADLLGIDSWA LVIGASMGGH RVLEWAATAP DRVDAIAAIA
TCAQTSGDQI AGFHTQLAAI QADPRYRDGD YYDAPDGEGP HVGLGLARQI AHQTYRSSVE
LDTRFGRIPQ GAEDPLEGGR FAVQSYLDHH GDKLARRFDA NSYVTLTRTM ITHDLGRDRG
GVEAALGQVT ARALVIAVDS DRLFTPAQSE RVAAAIPGAG PVRYVHSDYG HDGFLIEEDQ
VGRHVADFLR EGVRTR
//
