A0A3D5IUN2 · A0A3D5IUN2_9FLAO
- ProteinRiboflavin biosynthesis protein RibD
- GeneribD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids348 (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 + H2O + H+ = 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 | 53 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 55 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 80 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 89 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 159 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 178 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 192 | substrate | ||||
Sequence: R | ||||||
Binding site | 204 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 208 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 212 | substrate | ||||
Sequence: L | ||||||
Binding site | 215 | substrate | ||||
Sequence: R | ||||||
Binding site | 291 | substrate | ||||
Sequence: E | ||||||
Binding site | 293-299 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GLQTLQS |
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 > Zunongwangia
Accessions
- Primary accessionA0A3D5IUN2
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-128 | CMP/dCMP-type deaminase | ||||
Sequence: NIHEKYIKRCLQLAENGLGSTYPNPMVGSVIVYKNQIIGEGWHQKAGEPHAEVNAVNSVKNRDLLKKSTIYVSLEPCSHFGKTPPCSDLIIAKGIKKVVVATVDPFAEVAGRGIKKLMEAGCDVT |
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
- Length348
- Mass (Da)38,962
- Last updated2019-01-16 v1
- Checksum6B1C778ED35742FE