A0A7L5UF69 · A0A7L5UF69_9LACO
- ProteinRiboflavin biosynthesis protein RibD
- GeneribD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids351 (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 | 51 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 53 | Proton donor | |||
Binding site | 77 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 86 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 156 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 185 | substrate | |||
Binding site | 197 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 201 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 205 | substrate | |||
Binding site | 288 | substrate | |||
Binding site | 290-296 | NADP+ (UniProtKB | ChEBI) | |||
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 > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus
Accessions
- Primary accessionA0A7L5UF69
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 2-125 | CMP/dCMP-type deaminase | |||
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
- Length351
- Mass (Da)38,579
- Last updated2021-04-07 v1
- MD5 ChecksumCDA382E7FC1978E6396784FD0B1DA7D2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP047410 EMBL· GenBank· DDBJ | QLL69106.1 EMBL· GenBank· DDBJ | Genomic DNA |