Q55BH9 · DGAT1_DICDI
- ProteinDiacylglycerol O-acyltransferase 1
- Genedgat1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids617 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates.
Catalytic activity
- an acyl-CoA + a 1,2-diacyl-sn-glycerol = a triacyl-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- 2-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoyl-CoA = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + (9Z)-octadecenoyl-CoA = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- 1-O-(9Z-octadecenyl)-glycerol + (9Z)-octadecenoyl-CoA = 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoyl-CoA = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoyl-CoA = 1,2-di-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+ = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2OThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + (9Z)-octadecenoyl-CoA = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-dihexadecanoyl-1,2-hexadecanediol + 2 CoAThis reaction proceeds in the forward direction.
- hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- hexadecan-1-ol + hexadecanoyl-CoA = hexadecanyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- 13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- 1,3-di-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoyl-CoA = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- 2,3-di-(9Z)-octadecenoyl-sn-glycerol + (9Z)-octadecenoyl-CoA = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; glycerolipid metabolism.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 532 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | diacylglycerol O-acyltransferase activity | |
Molecular Function | retinol O-fatty-acyltransferase activity | |
Biological Process | ether lipid biosynthetic process | |
Biological Process | glycerol metabolic process | |
Biological Process | lipid droplet formation | |
Biological Process | monoacylglycerol biosynthetic process | |
Biological Process | triglyceride biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDiacylglycerol O-acyltransferase 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Dictyostelium
Accessions
- Primary accessionQ55BH9
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 217-237 | Helical | ||||
Sequence: LLLILLITASFRLVILNHLLY | ||||||
Transmembrane | 254-274 | Helical | ||||
Sequence: WPGVMISLMINLFIIAAYLIE | ||||||
Transmembrane | 306-326 | Helical | ||||
Sequence: IIAFSPNPASGIIVMILICTF | ||||||
Transmembrane | 399-419 | Helical | ||||
Sequence: IVEALSLSLLILWMVNQYMLP | ||||||
Transmembrane | 449-469 | Helical | ||||
Sequence: YVWLLGFYVFFHLYLNIVAEI | ||||||
Transmembrane | 520-540 | Helical | ||||
Sequence: GYFMCFFVSAIFHELVISIPF | ||||||
Transmembrane | 545-565 | Helical | ||||
Sequence: LWGFFGIMSQMVLIALTKNLM | ||||||
Transmembrane | 570-590 | Helical | ||||
Sequence: LGNVIFWISIVLGQPLVVLLY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000377488 | 1-617 | Diacylglycerol O-acyltransferase 1 | |||
Sequence: MEPIPPSNGNKNNSMDKQPQQPQQPQQQQQQQQQQRRDQRNSKLNELNETERVRNRFISHEFHKLDRTKSRIDAPKISFSDSESESDSEFFLAKRNTNNNNQNNTSPTFSSANGKQSNLTQRKINTQIQSKQPTNNNVQPLTDDEGTINHSNHHHHHHNQNNNGNNNNNNNNNNNNNKISTPPKQEEKMTMNGLFTLRPSILSSESNGSSYRGFLNLLLILLITASFRLVILNHLLYGIRINLDLYKISEYHRWPGVMISLMINLFIIAAYLIEKAAAKQLLPDRICYLLRIINCAAVIIVPSGSIIAFSPNPASGIIVMILICTFSMKIISYAYENSKQRKLNPDNKKFVIDPTNTSIYPNNLSLRSTYWFMLVPTLVYQLSYPRSPKIRKGYLLRRIVEALSLSLLILWMVNQYMLPLVQNSIEPLEKIDIVLIVERIMKLSLPNLYVWLLGFYVFFHLYLNIVAEITRFGDREFYRDWWNSTGLDYFWRTWNMPVHHWMVVLIYTPMRRRGFSKNMGYFMCFFVSAIFHELVISIPFHSLKLWGFFGIMSQMVLIALTKNLMNGRNLGNVIFWISIVLGQPLVVLLYYRNFVLENPEWYRNVEPPTSPPVMPFY |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-38 | Polar residues | ||||
Sequence: MEPIPPSNGNKNNSMDKQPQQPQQPQQQQQQQQQQRRD | ||||||
Region | 1-52 | Disordered | ||||
Sequence: MEPIPPSNGNKNNSMDKQPQQPQQPQQQQQQQQQQRRDQRNSKLNELNETER | ||||||
Compositional bias | 95-146 | Polar residues | ||||
Sequence: RNTNNNNQNNTSPTFSSANGKQSNLTQRKINTQIQSKQPTNNNVQPLTDDEG | ||||||
Region | 95-186 | Disordered | ||||
Sequence: RNTNNNNQNNTSPTFSSANGKQSNLTQRKINTQIQSKQPTNNNVQPLTDDEGTINHSNHHHHHHNQNNNGNNNNNNNNNNNNNKISTPPKQE | ||||||
Compositional bias | 161-186 | Polar residues | ||||
Sequence: NNNGNNNNNNNNNNNNNKISTPPKQE | ||||||
Motif | 477-483 | FYXDWWN motif | ||||
Sequence: FYRDWWN |
Sequence similarities
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length617
- Mass (Da)71,946
- Last updated2009-06-16 v2
- ChecksumDCD8FD193A3023D7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-38 | Polar residues | ||||
Sequence: MEPIPPSNGNKNNSMDKQPQQPQQPQQQQQQQQQQRRD | ||||||
Compositional bias | 95-146 | Polar residues | ||||
Sequence: RNTNNNNQNNTSPTFSSANGKQSNLTQRKINTQIQSKQPTNNNVQPLTDDEG | ||||||
Compositional bias | 161-186 | Polar residues | ||||
Sequence: NNNGNNNNNNNNNNNNNKISTPPKQE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAFI02000006 EMBL· GenBank· DDBJ | EAL71801.2 EMBL· GenBank· DDBJ | Genomic DNA |