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ECOLI:RIR1

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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

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10660
EcoGene:EG20257
MGI:MGI:98180
PANTHER:PTN000171388
SGD:S000000872
SGD:S000001328
UniProtKB:P9WH75

P

Seeded From UniProt

complete

part_of

GO:0005971

ribonucleoside-diphosphate reductase complex

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10660
EcoGene:EG20257
MGI:MGI:98180
PANTHER:PTN000171388
PomBase:SPAC1F7.05
SGD:S000000872
UniProtKB:P9WH75
UniProtKB:Q9I4I1

C

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10660
EcoGene:EG20257
MGI:MGI:98180
PANTHER:PTN000171388
SGD:S000000872
SGD:S000001328
UniProtKB:P9WH75
UniProtKB:Q08698

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22160671[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00452

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17726094[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00452

F

Seeded From UniProt

complete

involved_in

GO:0015949

nucleobase-containing small molecule interconversion

PMID:13973714[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009263

deoxyribonucleotide biosynthetic process

PMID:13973714[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005971

ribonucleoside-diphosphate reductase complex

PMID:13973714[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:4902211[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

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

PMID:357894[7]

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

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013509

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013509

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000788
InterPro:IPR013509

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000788
InterPro:IPR013346
InterPro:IPR013509

P

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.17.4.1

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0235
UniPathway:UPA00326

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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
  2. 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
  3. 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. 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
  5. 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
  6. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  7. Thelander, L et al. (1978) Ribonucleoside diphosphate reductase (Escherichia coli). Meth. Enzymol. 51 227-37 PubMed GONUTS page