A0AAD5BM78 · A0AAD5BM78_AMBAR
- Proteinxanthine dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1304 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Catalytic activity
- xanthine + NAD+ + H2O = urate + NADH + H+
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 52 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 57 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 60 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 82 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 122 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 125 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 158 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 160 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 287-294 | FAD (UniProtKB | ChEBI) | |||
Binding site | 367 | FAD (UniProtKB | ChEBI) | |||
Binding site | 377-381 | FAD (UniProtKB | ChEBI) | |||
Binding site | 390 | FAD (UniProtKB | ChEBI) | |||
Binding site | 434 | FAD (UniProtKB | ChEBI) | |||
Binding site | 452 | FAD (UniProtKB | ChEBI) | |||
Binding site | 798 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 829 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 833 | substrate | |||
Binding site | 911 | substrate | |||
Binding site | 943 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 945 | substrate | |||
Binding site | 1041 | substrate | |||
Binding site | 1110 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
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
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namexanthine dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Asteroideae > Heliantheae alliance > Heliantheae > Ambrosia
Accessions
- Primary accessionA0AAD5BM78
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length1,304
- Mass (Da)143,658
- Last updated2024-05-29 v1
- Checksum63A323EC35750FC8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAMZMK010011818 EMBL· GenBank· DDBJ | KAI7725930.1 EMBL· GenBank· DDBJ | Genomic DNA |