A0A4U0ZNL7 · A0A4U0ZNL7_9BACT
- ProteinRiboflavin biosynthesis protein RibD
- GeneribD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids362 (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 | 44 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 46 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 69 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 78 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 148 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 162 | substrate | ||||
Sequence: S | ||||||
Binding site | 164 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 178 | substrate | ||||
Sequence: R | ||||||
Binding site | 190 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 194 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 198 | substrate | ||||
Sequence: L | ||||||
Binding site | 201 | substrate | ||||
Sequence: R | ||||||
Binding site | 217 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 289 | substrate | ||||
Sequence: E | ||||||
Binding site | 291-297 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GGLLHGS |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity | |
Molecular Function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity | |
Molecular Function | NADP binding | |
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 > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfocapsaceae > Desulforhopalus
Accessions
- Primary accessionA0A4U0ZNL7
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-117 | CMP/dCMP-type deaminase | ||||
Sequence: MKLALKEAKKGIGRTSPNPAVGAVIVKDGVVVGRGYHQKAGTPHAEIHAINNARIPLQGATIYVTLEPCSHTGKTPPCCAAIEKAGINRVVVGMRDPNPLVDGRGLKYLRDHGIDVE |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)39,588
- Last updated2019-07-31 v1
- Checksum707E93894AC58384
Keywords
- Technical term