WSD_ACIAD
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 03-AUG-2022, entry version 113.
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; Proteobacteria; 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}.
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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; 62977.ACIAD0832; -.
DR EnsemblBacteria; CAG67733; CAG67733; ACIAD0832.
DR GeneID; 45233297; -.
DR KEGG; aci:ACIAD0832; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_024186_4_1_6; -.
DR OMA; FQPTFRK; -.
DR OrthoDB; 279287at2; -.
DR BioCyc; ASP62977:ACIAD_RS03845-MON; -.
DR BioCyc; MetaCyc:ACIAD0832-MON; -.
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 PANTHER; PTHR31650; PTHR31650; 1.
DR Pfam; PF03007; WES_acyltransf; 1.
DR Pfam; PF06974; WS_DGAT_C; 1.
DR TIGRFAMs; TIGR02946; acyl_WS_DGAT; 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"
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
