A0A2T5XY18 · A0A2T5XY18_9FLAO
- ProteinRiboflavin biosynthesis protein RibD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids350 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic activity
- 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H+ + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4+
Cofactor
Note: Binds 1 zinc ion.
Pathway
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 50 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 52 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 77 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 86 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 156 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 175 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 189 | substrate | ||||
Sequence: R | ||||||
Binding site | 201 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 205 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 209 | substrate | ||||
Sequence: L | ||||||
Binding site | 212 | substrate | ||||
Sequence: R | ||||||
Binding site | 291 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity | |
Molecular Function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity | |
Molecular Function | zinc ion binding | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRiboflavin biosynthesis protein RibD
Including 2 domains:
- Recommended nameDiaminohydroxyphosphoribosylaminopyrimidine deaminase
- EC number
- Short namesDRAP deaminase
- Alternative names
- Recommended name5-amino-6-(5-phosphoribosylamino)uracil reductase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Capnocytophaga
Accessions
- Primary accessionA0A2T5XY18
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-125 | CMP/dCMP-type deaminase | ||||
Sequence: MTDQQYIHRCIQLAQNGLGTTYPNPVVGSVIVYKDRVIGEGWHVRAGEAHAEVRAIASVKDKQLLSQSTLYVSLEPCSHYGKTPPCADLIIAHRIPRVVIGCTDPFAKVAGRGIQKLREAGCEVV |
Sequence similarities
In the C-terminal section; belongs to the HTP reductase family.
In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length350
- Mass (Da)39,328
- Last updated2018-07-18 v1
- Checksum4D22C58BDB4C1C54