B8AL89 · B8AL89_ORYSI
- ProteinUncharacterized protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1350 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Note: Binds 2 [2Fe-2S] clusters.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 49 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 54 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 57 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 79 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 119 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 122 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 167 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 169 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 373 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 413 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 433 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 801 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 832 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 939 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1113 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 1285 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionB8AL89
Proteomes
Genome annotation databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-97 | 2Fe-2S ferredoxin-type | ||||
Sequence: RAVVVAVNGERYEAVGVDPSTTLLEFLRTRTPVRGPKLGCGEGGCGACVVVVSKYDAVADEVTEFSASSCLTLLGSLHHCAVTTSEGI | ||||||
Domain | 245-437 | FAD-binding PCMH-type | ||||
Sequence: VVVTGDGWFHPKSVEEFHRLFDSNLFDERSVKIVASNTGSGVYKDQDLHEKYINISQIPELSAINRSSKGVEIGAVVSISQAIDILSDGGAVFRKIADHLSKVASPFVRNTATIGGNIIMAQRLSFSSDIATVLLAAGSTVTIQVAAKRMCITLEEFLKQPPCDSRTLLVSISIPDWGSDDGITFRTFRAAPR | ||||||
Region | 552-576 | Disordered | ||||
Sequence: NGSFTNGTANGIVDSSPEKHSNVDS |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,350
- Mass (Da)144,775
- Last updated2009-03-03 v1
- ChecksumD2BD3E28B16364E1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM000128 EMBL· GenBank· DDBJ | EEC76311.1 EMBL· GenBank· DDBJ | Genomic DNA |