Q9LEM9 · DES6_CERPU
- ProteinAcyl-lipid (9-3)-desaturase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids520 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Fatty acid desaturase able to introduce a delta6-double bond into delta9-unsaturated fatty-acid substrates. Has a strong preference for linoleic acid (18:2(9Z,12Z)).
Catalytic activity
- (9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + O2 + 2 H+ = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O
CHEBI:90078 + 2 RHEA-COMP:10438 + CHEBI:15379 + 2 CHEBI:15378 = CHEBI:90079 + 2 RHEA-COMP:10439 + 2 CHEBI:15377
Pathway
Lipid metabolism; polyunsaturated fatty acid biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water | |
Biological Process | unsaturated fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcyl-lipid (9-3)-desaturase
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Bryophyta > Bryophytina > Bryopsida > Dicranidae > Pseudoditrichales > Ditrichaceae > Ceratodon
Accessions
- Primary accessionQ9LEM9
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 22-42 | Helical | ||||
Sequence: LATMPLVSDFLNVLGTTLGQW | ||||||
Transmembrane | 203-223 | Helical | ||||
Sequence: YLFKTLINVSIVATSIAIISL | ||||||
Transmembrane | 229-249 | Helical | ||||
Sequence: AVLLSASLMGLFIQQCGWLSH | ||||||
Transmembrane | 261-281 | Helical | ||||
Sequence: WLNDVVGYVVGNVVLGFSVSW | ||||||
Transmembrane | 337-357 | Helical | ||||
Sequence: LFFLVLLTFARASWLFWSAAF | ||||||
Transmembrane | 373-393 | Helical | ||||
Sequence: GTMALHYIWFNSVAFYLLPGW | ||||||
Transmembrane | 396-416 | Helical | ||||
Sequence: VVWMVVSELMSGFLLGYVFVL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435459 | 1-520 | Acyl-lipid (9-3)-desaturase | |||
Sequence: MVSQGGGLSQGSIEENIDVEHLATMPLVSDFLNVLGTTLGQWSLSTTFAFKRLTTKKHSSDISVEAQKESVARGPVENISQSVAQPIRRRWVQDKKPVTYSLKDVASHDMPQDCWIIIKEKVYDVSTFAEQHPGGTVINTYFGRDATDVFSTFHASTSWKILQNFYIGNLVREEPTLELLKEYRELRALFLREQLFKSSKSYYLFKTLINVSIVATSIAIISLYKSYRAVLLSASLMGLFIQQCGWLSHDFLHHQVFETRWLNDVVGYVVGNVVLGFSVSWWKTKHNLHHAAPNECDQKYTPIDEDIDTLPIIAWSKDLLATVESKTMLRVLQYQHLFFLVLLTFARASWLFWSAAFTLRPELTLGEKLLERGTMALHYIWFNSVAFYLLPGWKPVVWMVVSELMSGFLLGYVFVLSHNGMEVYNTSKDFVNAQIASTRDIKAGVFNDWFTGGLNRQIEHHLFPTMPRHNLNKISPHVETLCKKHGLVYEDVSMASGTYRVLKTLKDVADAASHQQLAAS |
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 97-171 | Cytochrome b5 heme-binding | ||||
Sequence: PVTYSLKDVASHDMPQDCWIIIKEKVYDVSTFAEQHPGGTVINTYFGRDATDVFSTFHASTSWKILQNFYIGNLV | ||||||
Motif | 249-253 | Histidine box-1 | ||||
Sequence: HDFLH | ||||||
Motif | 286-290 | Histidine box-2 | ||||
Sequence: HNLHH | ||||||
Motif | 457-461 | Histidine box-3 | ||||
Sequence: QIEHH |
Domain
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence similarities
Belongs to the fatty acid desaturase type 1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length520
- Mass (Da)59,160
- Last updated2000-10-01 v1
- Checksum5A9332EECC153439