P07071 · NRDD_BPT4
- ProteinAnaerobic ribonucleoside-triphosphate reductase
- GenenrdD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids605 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Catalytic activity
- a ribonucleoside 5'-triphosphate + formate + H+ = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Activity regulation
Activated under anaerobic conditions by NrdG, a tightly associated activase. Activation involves the formation of a glycyl radical at Gly-580.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | dCTP 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 64 | dGTP 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 66 | dCTP 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 66 | dGTP 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 67 | dGTP 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 100 | dATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 100 | dCTP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 100 | dGTP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 100 | dTTP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 103 | dATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 103 | dCTP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 103 | dGTP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | dATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 114 | dCTP 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 114 | dTTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 146 | dATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 146 | dCTP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 146 | dGTP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 146 | dTTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 445-448 | dCTP 1 (UniProtKB | ChEBI) | ||||
Sequence: AENL | ||||||
Binding site | 447 | dGTP 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 448 | dGTP 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 543 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 546 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 561 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 564 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | anaerobic ribonucleoside-triphosphate reductase complex | |
Molecular Function | metal ion binding | |
Molecular Function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor | |
Molecular Function | ribonucleoside-triphosphate reductase (thioredoxin) activity | |
Biological Process | 2'-deoxyribonucleotide biosynthetic process | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnaerobic ribonucleoside-triphosphate reductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Straboviridae > Tevenvirinae > Tequatrovirus
- Virus hosts
Accessions
- Primary accessionP07071
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 580 | Lacks both glycyl radical and activity. Does not affect interaction with NrdG. | ||||
Sequence: G → A |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000166686 | 1-605 | Anaerobic ribonucleoside-triphosphate reductase | |||
Sequence: MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHESGIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVASHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEYEVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEEGVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDSTGNEILDGRNNLGVVTLNLPRIALDSYIGTQFNEQKFVELFNERMDLCFEALMCRISSLKGVKATVAPILYQEGAFGVRLKPDDDIIELFKNGRSSVSLGYIGIHELNILVGRDIGREILTKMNAHLKQWTERTGFAFSLYSTPAENLCYRFCKLDTEKYGSVKDVTDKGWYTNSFHVSVEENITPFEKISREAPYHFIATGGHISYVELPDMKNNLKGLEAVWDYAAQHLDYFGVNMPVDKCFTCGSTHEMTPTENGFVCSICGETDPKKMNTIRRTCGYLGNPNERGFNLGKNKEIMHRVKHQ | ||||||
Modified residue | 580 | Glycine radical | ||||
Sequence: G |
Keywords
- PTM
Interaction
Subunit
Homodimer. Forms a tetramer composed of two NrdD and two NrdG subunits.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 482-605 | Glycine radical | ||||
Sequence: ENITPFEKISREAPYHFIATGGHISYVELPDMKNNLKGLEAVWDYAAQHLDYFGVNMPVDKCFTCGSTHEMTPTENGFVCSICGETDPKKMNTIRRTCGYLGNPNERGFNLGKNKEIMHRVKHQ |
Sequence similarities
Belongs to the anaerobic ribonucleoside-triphosphate reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length605
- Mass (Da)67,957
- Last updated2002-01-23 v4
- ChecksumC5F29CE03126800B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y00122 EMBL· GenBank· DDBJ | CAA68308.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y00122 EMBL· GenBank· DDBJ | CAA68310.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AF158101 EMBL· GenBank· DDBJ | AAD42633.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X12629 EMBL· GenBank· DDBJ | CAA31150.1 EMBL· GenBank· DDBJ | Genomic DNA |