A0A9D1HE00 · A0A9D1HE00_9FIRM
- ProteinPhosphopentomutase
- GenedeoB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids397 (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 | 14 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 289 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 294 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 330 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 331 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 342 | 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 | 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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Candidatus Onthocola
Accessions
- Primary accessionA0A9D1HE00
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-381 | Metalloenzyme | ||||
Sequence: KRIFVIVIDSLGIGAMPDAADYGDEGADTLGHISEAADTFVIPHLQSLGLANLHPLKQVPPVERPLGYHMALREMSVSKDTMTGHWEMMGLNIRTPFRTFTEHGFPKELIEELERRTGHKVIGNKSASGTEIIEELGEEEIRTGHMIVYTSADSVLQICGNEETFGLDELYRCCEIARELTMKEEWKVGRVIARPYVGRKKGEFRRTANRHDYALKPFGRTALNALNDGGYDVLSVGKIQDIFQGEGITWAVRSKSSVEGMEQTIALTERDFHGLCYVNLVDFDALWGHRRNPKGYKEELERFDVRLGDLLEQLKDDDLLMITADHGTDPTYKGTDHTREKVPLLIYSPSMKQGGLLPEQETFAVIGATVADNFHV |
Sequence similarities
Belongs to the phosphopentomutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)44,437
- Last updated2023-05-03 v1
- Checksum6E00B784EE2D8FAD