ID WSD_ACIAD Reviewed; 458 AA. AC Q8GGG1; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 120. DE RecName: Full=O-acyltransferase WSD; DE AltName: Full=Diacylglycerol O-acyltransferase; DE Short=DGAT; DE EC=2.3.1.20; DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase; DE EC=2.3.1.75; DE AltName: Full=Wax ester synthase/acyl-CoA:diacylglycerol acyltransferase; DE AltName: Full=Wax synthase; DE Short=WS; GN Name=wax-dgaT; OrderedLocusNames=ACIAD0832; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, RP EXPRESSION IN OTHER BACTERIA, AND DISRUPTION PHENOTYPE. RX PubMed=12502715; DOI=10.1074/jbc.m210533200; RA Kalscheuer R., Steinbuchel A.; RT "A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol RT acyltransferase mediates wax ester and triacylglycerol biosynthesis in RT Acinetobacter calcoaceticus ADP1."; RL J. Biol. Chem. 278:8075-8082(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, RT a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: Bifunctional wax ester synthase/diacylglycerol CC acyltransferase (WS and DGAT). Catalyzes the terminal and only CC committed step in triacylglycerol synthesis by using diacylglycerol and CC fatty acyl CoA as substrates. Required for storage lipid synthesis. WS CC uses C(12)-CoA to C(18)-CoA substrates whereas DGAT prefers C(20)-CoA. CC Upon expression in E.coli and Pseudomonas citronellolis (DSM 50332) CC both WS and DGAT activities increase. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester + CC CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15.6 uM for palmitoyl-CoA (C(16), in wax synthase) CC {ECO:0000269|PubMed:12502715}; CC KM=21.1 uM for palmitoyl-CoA (diacylglycerol acyltransferase) CC {ECO:0000269|PubMed:12502715}; CC Vmax=212.8 pmol/min/mg enzyme (wax synthase) CC {ECO:0000269|PubMed:12502715}; CC Vmax=54.3 pmol/min/mg enzyme (diacylglycerol acyltransferase) CC {ECO:0000269|PubMed:12502715}; CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not make wax ester and CC only trace amounts of triacylglycerol. {ECO:0000269|PubMed:12502715}. CC -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family. CC {ECO:0000305}. 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; AF529086; AAO17391.1; -; Genomic_DNA. DR EMBL; CR543861; CAG67733.1; -; Genomic_DNA. DR RefSeq; WP_004922247.1; NC_005966.1. DR PDB; 7NXG; X-ray; 1.95 A; A=1-458. DR PDBsum; 7NXG; -. DR AlphaFoldDB; Q8GGG1; -. DR SMR; Q8GGG1; -. DR STRING; 202950.GCA_001485005_02586; -. DR GeneID; 45233297; -. DR KEGG; aci:ACIAD0832; -. DR eggNOG; COG1020; Bacteria. DR HOGENOM; CLU_024186_4_1_6; -. DR OrthoDB; 9810950at2; -. DR BioCyc; ASP62977:ACIAD_RS03845-MONOMER; -. DR BioCyc; MetaCyc:ACIAD0832-MONOMER; -. DR BRENDA; 2.3.1.20; 8909. DR BRENDA; 2.3.1.75; 8909. DR SABIO-RK; Q8GGG1; -. DR UniPathway; UPA00282; -. DR Proteomes; UP000000430; Chromosome. DR GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0047196; F:long-chain-alcohol O-fatty-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 InterPro; IPR014292; Acyl_transf_WS/DGAT. 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. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Glycerol metabolism; Lipid biosynthesis; KW Lipid metabolism; Reference proteome; Transferase. FT CHAIN 1..458 FT /note="O-acyltransferase WSD" FT /id="PRO_0000393350" FT ACT_SITE 133 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT STRAND 1..3 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 6..13 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 22..30 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:7NXG" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 79..83 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 90..101 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 111..120 FT /evidence="ECO:0007829|PDB:7NXG" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 124..132 FT /evidence="ECO:0007829|PDB:7NXG" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 138..148 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 234..242 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 243..253 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 257..275 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 305..309 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 317..330 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 340..351 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 388..396 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 405..412 FT /evidence="ECO:0007829|PDB:7NXG" FT STRAND 415..423 FT /evidence="ECO:0007829|PDB:7NXG" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:7NXG" FT TURN 428..431 FT /evidence="ECO:0007829|PDB:7NXG" FT HELIX 432..450 FT /evidence="ECO:0007829|PDB:7NXG" SQ SEQUENCE 458 AA; 51780 MW; AEFB9A1C83FE3823 CRC64; MRPLHPIDFI FLSLEKRQQP MHVGGLFLFQ IPDNAPDTFI QDLVNDIRIS KSIPVPPFNN KLNGLFWDED EEFDLDHHFR HIALPHPGRI RELLIYISQE HSTLLDRAKP LWTCNIIEGI EGNRFAMYFK IHHAMVDGVA GMRLIEKSLS HDVTEKSIVP PWCVEGKRAK RLREPKTGKI KKIMSGIKSQ LQATPTVIQE LSQTVFKDIG RNPDHVSSFQ APCSILNQRV SSSRRFAAQS FDLDRFRNIA KSLNVTINDV VLAVCSGALR AYLMSHNSLP SKPLIAMVPA SIRNDDSDVS NRITMILANL ATHKDDPLQR LEIIRRSVQN SKQRFKRMTS DQILNYSAVV YGPAGLNIIS GMMPKRQAFN LVISNVPGPR EPLYWNGAKL DALYPASIVL DGQALNITMT SYLDKLEVGL IACRNALPRM QNLLTHLEEE IQLFEGVIAK QEDIKTAN //