Q55406 · DESC_SYNY3
- Proteinsn-1 stearoyl-lipid 9-desaturase
- GenedesC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids318 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Desaturase involved in fatty acid biosynthesis (PubMed:7929259, PubMed:8419301).
Introduces a double bond at carbon 9 of stearoyl groups (18:0) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids (PubMed:7929259).
Does not desaturate palmitic acid (16:0), palmitoleic acid (16:1) and cis-vaccenic acid (18:1) (PubMed:7929259).
Introduces a double bond at carbon 9 of stearoyl groups (18:0) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids (PubMed:7929259).
Does not desaturate palmitic acid (16:0), palmitoleic acid (16:1) and cis-vaccenic acid (18:1) (PubMed:7929259).
Catalytic activity
- a 1-octadecanoyl 2-acyl-glycerolipid + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H+ = a 1-[(9Z)-octadecenoyl]-2-acyl-glycerolipid + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 H2OThis reaction proceeds in the forward direction.
CHEBI:87007 + 2 RHEA-COMP:10001 + CHEBI:15379 + 2 CHEBI:15378 = CHEBI:87008 + 2 RHEA-COMP:10000 + 2 CHEBI:15377
Cofactor
Pathway
Lipid metabolism; polyunsaturated fatty acid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane-derived thylakoid membrane | |
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 namesn-1 stearoyl-lipid 9-desaturase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Merismopediaceae > Synechocystis
Accessions
- Primary accessionQ55406
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cellular thylakoid membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 56-76 | Helical | ||||
Sequence: VIFFFTSIHLVALLAFLPQFF | ||||||
Transmembrane | 80-100 | Helical | ||||
Sequence: AVGMAFLLYVITGGIGITLGF | ||||||
Transmembrane | 117-137 | Helical | ||||
Sequence: YIFVICGTLACQGGVFEWVGL | ||||||
Transmembrane | 201-221 | Helical | ||||
Sequence: VALGLILFALGGWPFVIWGIF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459818 | 1-318 | sn-1 stearoyl-lipid 9-desaturase | |||
Sequence: MLNPLNIEYLYLSKLFDNSLIVFNKRQLFRFFVRFFFMTAALPNDSKPKLTPAWTVIFFFTSIHLVALLAFLPQFFSWKAVGMAFLLYVITGGIGITLGFHRCISHRSFNVPKWLEYIFVICGTLACQGGVFEWVGLHRMHHKFSDTTPDPHDSNKGFWWSHIGWMMFEIPAKADIPRYTKDIQDDKFYQFCQNNLILIQVALGLILFALGGWPFVIWGIFVRLVFVFHFTWFVNSATHKFGYVSHESNDYSRNCWWVALLTFGEGWHNNHHAYQYSARHGLQWWEVDLTWMTIKFLSLLGLAKDIKLPPETAMANKA |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 101-106 | Histidine box-1 | ||||
Sequence: HRCISH | ||||||
Motif | 138-142 | Histidine box-2 | ||||
Sequence: HRMHH | ||||||
Motif | 271-275 | Histidine box-3 | ||||
Sequence: HHAYQ |
Domain
The histidine box domains are involved in binding the catalytic metal ions.
Sequence similarities
Belongs to the fatty acid desaturase type 2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length318
- Mass (Da)37,203
- Last updated1996-11-01 v1
- Checksum74DFD436B6567BF2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D16547 EMBL· GenBank· DDBJ | BAA03982.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BA000022 EMBL· GenBank· DDBJ | BAA10500.1 EMBL· GenBank· DDBJ | Genomic DNA |