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ECOLI:RIR1
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | nrdA (synonyms: dnaF) | |
| Protein Name(s) | Ribonucleoside-diphosphate reductase 1 subunit alpha
Protein B1 Ribonucleoside-diphosphate reductase 1 R1 subunit Ribonucleotide reductase 1 | |
| External Links | ||
| UniProt | P00452 | |
| EMBL | K02672 X06999 U00096 AP009048 | |
| PIR | H64993 | |
| RefSeq | NP_416737.1 WP_001075164.1 | |
| PDB | 1QFN 1R1R 1RLR 2R1R 2X0X 2XAK 2XAP 2XAV 2XAW 2XAX 2XAY 2XAZ 2XO4 2XO5 3R1R 3UUS 4ERM 4ERP 4R1R 5CNS 5CNT 5CNU 5CNV 5R1R 6R1R 7R1R | |
| PDBsum | 1QFN 1R1R 1RLR 2R1R 2X0X 2XAK 2XAP 2XAV 2XAW 2XAX 2XAY 2XAZ 2XO4 2XO5 3R1R 3UUS 4ERM 4ERP 4R1R 5CNS 5CNT 5CNU 5CNV 5R1R 6R1R 7R1R | |
| ProteinModelPortal | P00452 | |
| SMR | P00452 | |
| DIP | DIP-584N | |
| IntAct | P00452 | |
| MINT | MINT-1233906 | |
| STRING | 511145.b2234 | |
| EPD | P00452 | |
| PaxDb | P00452 | |
| PRIDE | P00452 | |
| EnsemblBacteria | AAC75294 BAA16053 | |
| GeneID | 946612 | |
| KEGG | ecj:JW2228 eco:b2234 | |
| PATRIC | 32119827 | |
| EchoBASE | EB0654 | |
| EcoGene | EG10660 | |
| eggNOG | ENOG4105BZH COG0209 | |
| HOGENOM | HOG000278076 | |
| InParanoid | P00452 | |
| KO | K00525 | |
| OMA | YELLWQM | |
| OrthoDB | EOG6J48HC | |
| PhylomeDB | P00452 | |
| BioCyc | EcoCyc:NRDA-MONOMER ECOL316407:JW2228-MONOMER MetaCyc:NRDA-MONOMER | |
| BRENDA | 1.17.4.1 | |
| SABIO-RK | P00452 | |
| UniPathway | UPA00326 | |
| EvolutionaryTrace | P00452 | |
| PRO | PR:P00452 | |
| Proteomes | UP000000318 UP000000625 | |
| GO | GO:0005829 GO:0005971 GO:0005524 GO:0004748 GO:0009263 GO:0006260 GO:0015949 | |
| InterPro | IPR005144 IPR013346 IPR000788 IPR013509 IPR008926 | |
| Pfam | PF03477 PF02867 PF00317 | |
| PRINTS | PR01183 | |
| SUPFAM | SSF48168 | |
| TIGRFAMs | TIGR02506 | |
| PROSITE | PS51161 PS00089 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0009263 |
deoxyribonucleotide biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10660 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005971 |
ribonucleoside-diphosphate reductase complex |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10660 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004748 |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10660 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0015949 |
nucleobase-containing small molecule interconversion |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009263 |
deoxyribonucleotide biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005971 |
ribonucleoside-diphosphate reductase complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004748 |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004748 |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006260 |
DNA replication |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004748 |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0008152 |
metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006260 |
DNA replication |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0235 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Ando, N et al. (2011) Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A. 108 21046-51 PubMed GONUTS page
- ↑ Wang, J et al. (2007) Enhanced subunit interactions with gemcitabine-5'-diphosphate inhibit ribonucleotide reductases. Proc. Natl. Acad. Sci. U.S.A. 104 14324-9 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 REICHARD, P (1962) Enzymatic synthesis of deoxyribonucleotides. I. Formation of deoxycytidine diphosphate from cytidine diphosphate with enzymes from Escherichia coli. J. Biol. Chem. 237 3513-9 PubMed GONUTS page
- ↑ Brown, NC & Reichard, P (1969) Ribonucleoside diphosphate reductase. Formation of active and inactive complexes of proteins B1 and B2. J. Mol. Biol. 46 25-38 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Thelander, L et al. (1978) Ribonucleoside diphosphate reductase (Escherichia coli). Meth. Enzymol. 51 227-37 PubMed GONUTS page
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