ID U5E762_NOCAS Unreviewed; 452 AA.
AC U5E762;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Diacylglycerol O-acyltransferase {ECO:0000256|ARBA:ARBA00013244, ECO:0000256|RuleBase:RU361241};
DE EC=2.3.1.20 {ECO:0000256|ARBA:ARBA00013244, ECO:0000256|RuleBase:RU361241};
GN ORFNames=NCAST_17_00970 {ECO:0000313|EMBL:GAD83115.1};
OS Nocardia asteroides NBRC 15531.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD83115.1, ECO:0000313|Proteomes:UP000017048};
RN [1] {ECO:0000313|EMBL:GAD83115.1, ECO:0000313|Proteomes:UP000017048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD83115.1,
RC ECO:0000313|Proteomes:UP000017048};
RX PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA Suzuki K., Fujita N., Gonoi T.;
RT "Genome based analysis of type-I polyketide synthase and nonribosomal
RT peptide synthetase gene clusters in seven strains of five representative
RT Nocardia species.";
RL BMC Genomics 15:323-323(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00001039,
CC ECO:0000256|RuleBase:RU361241};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004771, ECO:0000256|RuleBase:RU361241}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009587, ECO:0000256|RuleBase:RU361241}.
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:GAD83115.1}.
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DR EMBL; BAFO02000017; GAD83115.1; -; Genomic_DNA.
DR RefSeq; WP_019050018.1; NZ_VBUS01000001.1.
DR AlphaFoldDB; U5E762; -.
DR STRING; 1824.SAMN05444423_101444; -.
DR eggNOG; COG1020; Bacteria.
DR OrthoDB; 9810950at2; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000017048; Unassembled WGS sequence.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR014292; Acyl_transf_WS/DGAT.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR NCBIfam; TIGR02946; acyl_WS_DGAT; 1.
DR PANTHER; PTHR31650:SF1; DIACYGLYCEROL O-ACYLTRANSFERASE TGS4-RELATED; 1.
DR PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 1.
DR Pfam; PF06974; WS_DGAT_C; 1.
DR Pfam; PF03007; WS_DGAT_cat; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361241};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798,
KW ECO:0000256|RuleBase:RU361241};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU361241};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361241};
KW Reference proteome {ECO:0000313|Proteomes:UP000017048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361241}.
FT DOMAIN 5..261
FT /note="O-acyltransferase WSD1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03007"
FT DOMAIN 303..447
FT /note="O-acyltransferase WSD1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06974"
FT REGION 161..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 49608 MW; 44B7DEA06183DBEE CRC64;
MEFIAPLDAL FLLAESREHP MHVGSLHLFE PPEGAGPDYL REFRDALLAE QTLRPTFRKR
PATLLGAPQL AWTQDGEVDL DYHVQRSALP APGRMGQLLD HASKLHSALL DRHRPMWELH
FVEGLADGRF ALYSKMHHSL IDGVSAQRLL RRTLTTDQFD PELKKPWNLP RAQRPDRPRP
QRSRLGGLLG NLSSAGSSGA ALLRAARTGL VEQQLTLPFE APRTLFNVPI GGARKCVVRT
WSMDRIKQVK KATGTTVNDV VLAMSAGALR SYLLERDALP DKPMIALVPM SLRDAEDTDT
QGVKIAALLC NLGTDVADPL ERLRVVSEST RRNKEVYRSL TPTQTLAVAG LMLSPLAAML
LPGFASVGTP PFNIVISNVP GSRDPLYWNG ARLDASYPLS IPLDGQAVNI TLTSNGDNLD
FGLVGCRRTL PDLHRLLDHL EDSLAALEDA AA
//