A0A251SR47 · A0A251SR47_HELAN
- ProteinAldehyde oxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1346 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Note: Binds 2 [2Fe-2S] clusters.
Pathway
Alkaloid biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 55 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 60 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 63 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 85 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 125 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 128 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 172 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 174 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 358-362 | FAD (UniProtKB | ChEBI) | ||||
Sequence: SVGGN | ||||||
Binding site | 374 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 414 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 443 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 783 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 814 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 927 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1101 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 1277 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | electron transfer activity | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | alkaloid metabolic process | |
Biological Process | ferredoxin metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Asteroideae > Heliantheae alliance > Heliantheae > Helianthus
Accessions
- Primary accessionA0A251SR47
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-103 | 2Fe-2S ferredoxin-type | ||||
Sequence: QTLVFAVNGERVELTSVDPSTTLLQFLRSHTRFKSVKLGCGEGGCGACNVLLSKFDTKLKQLEDYTVSSCLTLLCSINGCSITTTEGL | ||||||
Domain | 236-424 | FAD-binding PCMH-type | ||||
Sequence: LNYQDKTWYSPVSVEELGSLLESISAENGMTVKLVAGNTGTGYYQETEYYNKYIDLRCIPELSEIKKAGSRIEIGATVSISKLIFALKEHTKDDPTKEDDVVLKKIASHLEKIASESIRNVASVGGNLVMAQRKNFPSDIATVLLAVNSRVTILTGVKKETLTLEEFLEKPALDSRNVLLSVFIPCLRP |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,346
- Mass (Da)146,928
- Last updated2017-11-22 v1
- ChecksumD5A3105CBF3584E4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MNCJ02000328 EMBL· GenBank· DDBJ | KAF5773183.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM007902 EMBL· GenBank· DDBJ | OTG01317.1 EMBL· GenBank· DDBJ | Genomic DNA |