A0A6A7XYU3 · A0A6A7XYU3_9HYPH
- ProteinPhosphopentomutase
- GenedeoB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 305 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 310 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 346 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 347 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 358 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 | nucleotide metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphopentomutase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Segnochrobactraceae > Segnochrobactrum
Accessions
- Primary accessionA0A6A7XYU3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-395 | Metalloenzyme | ||||
Sequence: RAFLLILDSVGIGASADAAHFGDAGADTVGHIAERCAAGAADRPGLRQGPLALPNLVALGLGRAVAASRGSPAPGLSSDVAPSGAWGYGIEVSSGKDTPSGHWEIAGVPVPFDWGYFPQTVPTFPPDLVAALISEAGLPGILGDRHASGTEIIAELGEESIRTGKPICYTSADSVFQIAAHEGHFGLDRLYRVCEIARRLVDPLNIGRVIARPFVGESRDTFVRTANRRDYAVPPPEPTLLDRAAGAGRAVIGIGKIGDIYAHRGVTEVVKAAGNDALFDATLAAADRAGEGDLVVTNFVDFDMVYGHRRDVPGYAAALEAFDRRLPTFTARMRPGDLAVITADHGCDPTFRGNDHTREHVPILAFGPGIAPRAIGPRATFADIGETLAAWLD |
Sequence similarities
Belongs to the phosphopentomutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length406
- Mass (Da)42,512
- Last updated2020-06-17 v1
- Checksum690F8CED95458AF7
Keywords
- Technical term