A0A1I0R311 · A0A1I0R311_9FIRM
- ProteinMultifunctional fusion protein
- GenedeoC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids610 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Isomerase that catalyzes the conversion of deoxy-ribose 1-phosphate (dRib-1-P) and ribose 1-phosphate (Rib-1-P) to deoxy-ribose 5-phosphate (dRib-5-P) and ribose 5-phosphate (Rib-5-P), respectively.
Catalytic activity
- 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Cofactor
Note: Binds 2 manganese ions.
Pathway
Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 1/2.
Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 296 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 332 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 333 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 344 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 489 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Active site | 553 | Schiff-base intermediate with acetaldehyde | ||||
Sequence: K | ||||||
Active site | 582 | Proton donor/acceptor | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | deoxyribose-phosphate aldolase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | phosphopentomutase activity | |
Biological Process | 2-deoxyribose 1-phosphate catabolic process | |
Biological Process | 5-phosphoribose 1-diphosphate biosynthetic process | |
Biological Process | cellular metabolic compound salvage | |
Biological Process | deoxyribonucleotide catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameDeoxyribose-phosphate aldolase
- EC number
- Short namesDERA
- Alternative names
- Recommended namePhosphopentomutase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae
Accessions
- Primary accessionA0A1I0R311
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-378 | Metalloenzyme | ||||
Sequence: KRVFIVVLDSFGIGLAPDAAAFGDEGSNTLAAVCSYSNDAFPNLARMGLWHIDGHDDSRITSWIDAQESLPSPIGSYGRIRELSAGKDSTIGHWEMAGVTSSKPLPTYPEGFPQEILDKLKKATGRDILCNKPYSGTDVIRDYGEEHMKTGALIVYTSADSVLQIAAHEDIVPVETLYEYCRSAREIMTGEHAVGRIIARPFTGEPGNFTRTPRRHDYSLEAPSATLNDVLKNEGLDVISVGKINDLFAGRGVTESNPTSGNTEGIAKLIEFMDRDFHGLCYVNLVDFDMKYGHRNDIEGYATAMHEFDDGLGKVLDLLNKDDLLIITADHGCDPSTESTDHSRECVPVLVYGEGHDVPHNLGYMAGFSHVANIAY |
Sequence similarities
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Belongs to the phosphopentomutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length610
- Mass (Da)65,061
- Last updated2017-11-22 v1
- ChecksumDD138DFC92E03617
Keywords
- Technical term