DGAT1_RAT
ID DGAT1_RAT Reviewed; 498 AA.
AC Q9ERM3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:O75907};
DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase;
DE Short=ARAT;
DE Short=Retinol O-fatty-acyltransferase;
DE EC=2.3.1.76;
DE AltName: Full=Diglyceride acyltransferase;
GN Name=Dgat1 {ECO:0000312|RGD:628673}; Synonyms=Dgat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway; TISSUE=Brain;
RA Zhang Y., Yang Q., Basse P., Rice P.;
RT "Cloning of a rat novel gene encoding an acyl CoA:diacylglycerol
RT acyltransferase, a key enzyme in triacylglycerol synthesis.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the terminal and only committed step in
CC triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as
CC substrates. Highly expressed in epithelial cells of the small intestine
CC and its activity is essential for the absorption of dietary fats. In
CC liver, plays a role in esterifying exogenous fatty acids to glycerol,
CC and is required to synthesize fat for storage (By similarity). Also
CC present in female mammary glands, where it produces fat in the milk (By
CC similarity). May be involved in VLDL (very low density lipoprotein)
CC assembly (By similarity). In contrast to DGAT2 it is not essential for
CC survival (By similarity). Functions as the major acyl-CoA retinol
CC acyltransferase (ARAT) in the skin, where it acts to maintain retinoid
CC homeostasis and prevent retinoid toxicity leading to skin and hair
CC disorders (By similarity). Exhibits additional acyltransferase
CC activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT),
CC wax monoester and wax diester synthases (By similarity). Also able to
CC use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis
CC of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
CC {ECO:0000250|UniProtKB:O75907, ECO:0000250|UniProtKB:Q8MK44,
CC ECO:0000250|UniProtKB:Q9Z2A7}.
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:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester +
CC CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000250|UniProtKB:O75907,
CC ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000250|UniProtKB:O75907,
CC ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-
CC (9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138734;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-mono-(9Z-
CC octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-
CC octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138734, ChEBI:CHEBI:138735;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+)
CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38380;
CC Evidence={ECO:0000250|UniProtKB:O75907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38307, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75728, ChEBI:CHEBI:75729;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38308;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-
CC dihexadecanoyl-1,2-hexadecanediol + 2 CoA; Xref=Rhea:RHEA:38211,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586,
CC ChEBI:CHEBI:75608; Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38212;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38171, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75587;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-
CC di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75583;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl
CC hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:55296, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:138722;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55297;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75824; Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440;
CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC -!- SUBUNIT: Homodimer or homotetramer; both forms have similar enzymatic
CC activities. {ECO:0000250|UniProtKB:O75907}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z2A7}.
CC -!- DOMAIN: The disordered N-terminal region is required for the
CC diacylglycerol O-acyltransferase activity and may regulate enzymatic
CC function via its interaction with the MBOAT fold.
CC {ECO:0000250|UniProtKB:O75907}.
CC -!- DOMAIN: The MBOAT fold forms a reaction chamber in the endoplasmic
CC reticulum membrane that encloses the active sites. The reaction chamber
CC has a tunnel to the cytosolic side and its entrance recognizes the
CC hydrophilic CoA motif of an acyl-CoA molecule. The chamber has separate
CC entrances for each of the two substrates, acyl-CoA and 1,2-diacyl-sn-
CC glycerol. {ECO:0000250|UniProtKB:O75907}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AF296131; AAG10084.1; -; mRNA.
DR RefSeq; NP_445889.1; NM_053437.1.
DR AlphaFoldDB; Q9ERM3; -.
DR SMR; Q9ERM3; -.
DR STRING; 10116.ENSRNOP00000035110; -.
DR BindingDB; Q9ERM3; -.
DR ChEMBL; CHEMBL6129; -.
DR PaxDb; Q9ERM3; -.
DR PeptideAtlas; Q9ERM3; -.
DR GeneID; 84497; -.
DR KEGG; rno:84497; -.
DR UCSC; RGD:628673; rat.
DR CTD; 8694; -.
DR RGD; 628673; Dgat1.
DR eggNOG; KOG0380; Eukaryota.
DR InParanoid; Q9ERM3; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; Q9ERM3; -.
DR BRENDA; 2.3.1.20; 5301.
DR Reactome; R-RNO-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00230; -.
DR PRO; PR:Q9ERM3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; ISO:RGD.
DR GO; GO:0016746; F:acyltransferase activity; IMP:RGD.
DR GO; GO:0019992; F:diacylglycerol binding; IDA:RGD.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:RGD.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:RGD.
DR GO; GO:0030073; P:insulin secretion; IMP:RGD.
DR GO; GO:1902224; P:ketone body metabolic process; IMP:RGD.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; IMP:RGD.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:RGD.
DR GO; GO:1903998; P:regulation of eating behavior; IMP:RGD.
DR GO; GO:1904729; P:regulation of intestinal lipid absorption; IMP:RGD.
DR GO; GO:1901738; P:regulation of vitamin A metabolic process; IMP:RGD.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:RGD.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:RGD.
DR InterPro; IPR027251; Diacylglycerol_acylTrfase1.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR PANTHER; PTHR10408; PTHR10408; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
DR PIRSF; PIRSF500231; Oat_dag; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..498
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000207656"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..127
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 128..139
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..165
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 166..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..193
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 194..200
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 201..232
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 233..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..319
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 320..326
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..364
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 365..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 411..431
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 432..439
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..458
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 459..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..492
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 493..498
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..96
FT /note="Involved in homomerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 128..139
FT /note="Extracellular loop 1 (EL1)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 140..498
FT /note="MBOAT fold"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 235..287
FT /note="Intracellular loop 1 (IL1)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 365..410
FT /note="Intracellular loop 2 (IL2)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 391..405
FT /note="Amphipathic helix (AH)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT MOTIF 371..377
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT ACT_SITE 426
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT BINDING 385..393
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 401
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 415
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 488
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT SITE 427
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75907"
SQ SEQUENCE 498 AA; 56870 MW; 5B24DD4AEB87CB4D CRC64;
MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVREAAVS PDLGAGGDAP APAPAPAHTR
DKDRQTSVGD GHWELRCHRL QDSLFSSDSG FSNYRGILNW CVVMLILSNA RLSLENLIKY
GILVDPIQVV SLFLKDPYSW PAPCLIIASN IFIVATFQIE KRLSVGALTE QMGLLLHVVN
LATIICFPAA VALLVESITP VGSLFALASY SIIFLKLSSY RDVNLWCRQR RVKAKAVSAG
KKVSGAAAQN TVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT
QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY WLFHSCLNAV
AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF YKPMLRLGSN KWMARTGVFW
ASAFFHEYLV SIPLRMFRLW AFTAMMAQVP LAWIVNRFFQ GNYGNAAVWV TLIIGQPVAV
LMYVHDYYVL NYDAPVGA
