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Database: UniProt
Entry: G7GLY9_9ACTN
LinkDB: G7GLY9_9ACTN
Original site: G7GLY9_9ACTN 
ID   G7GLY9_9ACTN            Unreviewed;       466 AA.
AC   G7GLY9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=GOAMR_20_01620 {ECO:0000313|EMBL:GAB04614.1};
OS   Gordonia amarae NBRC 15530.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB04614.1, ECO:0000313|Proteomes:UP000006023};
RN   [1] {ECO:0000313|EMBL:GAB04614.1, ECO:0000313|Proteomes:UP000006023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB04614.1,
RC   ECO:0000313|Proteomes:UP000006023};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:GAB04614.1}.
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DR   EMBL; BAED01000020; GAB04614.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7GLY9; -.
DR   STRING; 1075090.GOAMR_20_01620; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 9810950at2; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000006023; 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   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; 2.
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:UP000006023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361241}.
FT   DOMAIN          1..275
FT                   /note="O-acyltransferase WSD1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03007"
FT   DOMAIN          318..459
FT                   /note="O-acyltransferase WSD1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06974"
SQ   SEQUENCE   466 AA;  50686 MW;  BBB021B5D431E749 CRC64;
     MGPVDTIWLN MDTPENLMVI DSLMVLDGPA DWDRVSELFQ KRLVEAYPSF RQRVKRPRAG
     IGSPHWNHDP NFLLSKHLIR HTLPDGEDST LQRYIEEQMQ IPLRQTRPLW QAHLIDGYHK
     GSVIYSRIHH CIADGIALNE VMLSLTEATP DGDLPAEPAA GETPVDAQPS LVAQVQDAAD
     HGLEILTSAA RTVASVPSKF GPTAAIRAID QLTGALRQVA RTGDVADKLL LAEGAPQGPL
     TGTPGRSKRA VWCQPFALAD IKLLGRKTGT TVNDVLMCAM AGALGGYLEE HGADRGDLPT
     MVPVNVRTPG QAPPAELGNE FALVVVEYPT RLREPIERLM ETHRRMDAIK NSPEAFIVFS
     GIRVIGLTVK ELEKVLVGFF SSKATGVTTN VPGPREARYL GGSRIDGMLA WAPTAGDQTI
     AACIYTYNGQ VWVGFKADAD QVAEPEKLVS AFDAEVKELV RLAHAV
//
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