A0A2G9GKH2 · A0A2G9GKH2_9LAMI
- ProteinXanthine dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1366 (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 | 51 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 56 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 59 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 81 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 121 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 124 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 168 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 170 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 359-363 | FAD (UniProtKB | ChEBI) | ||||
Sequence: SLGGN | ||||||
Binding site | 375 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 444 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 802 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 833 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 946 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1120 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 1296 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | aldehyde oxidase activity | |
Molecular Function | electron transfer activity | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Bignoniaceae > Crescentiina > Tabebuia alliance > Handroanthus
Accessions
- Primary accessionA0A2G9GKH2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-99 | 2Fe-2S ferredoxin-type | ||||
Sequence: DSLVFEINGERFEVPEVDPSTTLLEFLRSRTRFKSVKLGCGEGGCGACVVLLSKYDPVSKQIESFSVSSCLTLLCSVNGCSITTSEGL | ||||||
Domain | 237-425 | FAD-binding PCMH-type | ||||
Sequence: LNFQKYSWYTPVTVEELQSLLNSNTVGSGERIKLVVGNTGDGYYKETEKYDKYIDLRYIPELSAVKKDNSGIEFGAALPISKVISYLKEESKLNSCSGGELVFTRVAEHMEKIASGFIRNSASLGGNLVMAQRKYFPSDIATLLLAVGSSVTILTHHKRETITIEDFLYRPPLDPKDVLLSVHIPLLKP |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,366
- Mass (Da)148,483
- Last updated2018-01-31 v1
- ChecksumBF7CC5DAD14EAD06
Keywords
- Technical term