O84735 · RIBD_CHLTR
- ProteinRiboflavin biosynthesis protein RibD
- GeneribD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids375 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 55 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 57 | 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 | 173 | substrate | ||||
Sequence: S | ||||||
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 | 230 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 299 | substrate | ||||
Sequence: E | ||||||
Binding site | 301-307 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GAQLHSA |
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
- Strain
- Taxonomic lineageBacteria > Chlamydiota > Chlamydiia > Chlamydiales > Chlamydiaceae > Chlamydia/Chlamydophila group > Chlamydia
Accessions
- Primary accessionO84735
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000171719 | 1-375 | Riboflavin biosynthesis protein RibD | |||
Sequence: MEVLSEQQLFFMRKAVALGEKGRIFAPPNPWVGCVIVKNGCVIGEGWHQGIGSPHAEVCAVQDQKCSLEGAEVFVTLEPCCHFGRTPPCVDLLIKSKVAAVYVGLLDPDPRVCKKGVARLQAAGIPVYVGVGSQEAKTSLQPYLYQRERGLPWVVMKTAASLDGQTADRGGSSQWISGELARADVGKLRAESQAIIVGARTVCLDNPRLSARFPHGDLYERQPLRVVVDSRGTVPLESRVFDLSSGSTLFATTQQCPKEYIQKLKDLGVEVWESSSHQVDLKGLLRYLAERGCLQVLVEGGAQLHSAFWQQKLVNAGVIYWGPKFLGDQGQPMLRDLQLSLVTAEHVRITETSLVRDSVKTCFECLEQESVDKKG |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-150 | Deaminase | ||||
Sequence: MEVLSEQQLFFMRKAVALGEKGRIFAPPNPWVGCVIVKNGCVIGEGWHQGIGSPHAEVCAVQDQKCSLEGAEVFVTLEPCCHFGRTPPCVDLLIKSKVAAVYVGLLDPDPRVCKKGVARLQAAGIPVYVGVGSQEAKTSLQPYLYQRERG | ||||||
Domain | 6-127 | CMP/dCMP-type deaminase | ||||
Sequence: EQQLFFMRKAVALGEKGRIFAPPNPWVGCVIVKNGCVIGEGWHQGIGSPHAEVCAVQDQKCSLEGAEVFVTLEPCCHFGRTPPCVDLLIKSKVAAVYVGLLDPDPRVCKKGVARLQAAGIPV | ||||||
Region | 151-375 | Reductase | ||||
Sequence: LPWVVMKTAASLDGQTADRGGSSQWISGELARADVGKLRAESQAIIVGARTVCLDNPRLSARFPHGDLYERQPLRVVVDSRGTVPLESRVFDLSSGSTLFATTQQCPKEYIQKLKDLGVEVWESSSHQVDLKGLLRYLAERGCLQVLVEGGAQLHSAFWQQKLVNAGVIYWGPKFLGDQGQPMLRDLQLSLVTAEHVRITETSLVRDSVKTCFECLEQESVDKKG |
Sequence similarities
In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
In the C-terminal section; belongs to the HTP reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)41,088
- Last updated1998-11-01 v1
- Checksum8E78F32BD73611E2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE001273 EMBL· GenBank· DDBJ | AAC68325.1 EMBL· GenBank· DDBJ | Genomic DNA |