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BPT4:RIR1

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Species (Taxon ID) Enterobacteria phage T4 (Bacteriophage T4). (10665)
Gene Name(s) NRDA
Protein Name(s) Ribonucleoside-diphosphate reductase subunit alpha

Protein B1 Ribonucleotide reductase

External Links
UniProt P32282
EMBL J03968
AF158101
M22627
RefSeq NP_049845.1
ProteinModelPortal P32282
GeneID 1258795
UniPathway UPA00326
Proteomes UP000009087
GO GO:0005524
GO:0004748
GO:0006260
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
GO:0005971

ribonucleoside-diphosphate reductase complex

PMID:809436[1]

ECO:0000314

C

Figure 4 shows that NrdA and NrdB from bacteriophage T4 have no activity alone; both are necessary to form a complex capable of ribonucleoside-diphosphate reductase activity

complete
CACAO 10851

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

PMID:1512207[2]

ECO:0000314

F

Both nrdA and nrdB were cleaved out of T4 phage genome. They were then put into a plasmid vector (pnrdAB)and implanted into E. coli N4830. Expression was induced by increasing temperature. Ribonucleoside diphosphate reductase was observed to increase in the E. coli strains containing the pnrdAB vector.

complete
CACAO 10953

GO:0055114

oxidation-reduction process

PMID:9309223[3]

ECO:0000314

P

Figure 2 shows allosteric substrate specificity site is occupied by the effector molecule dTTP.

complete
CACAO 11601

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

PMID:1512207[2]

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: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

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

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

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: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: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

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

Notes

References

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

  1. Berglund, O (1975) Ribonucleoside diphosphate reductase induced by bacteriophage T4. III. Isolation and characterization of proteins B1 and B2. J. Biol. Chem. 250 7450-5 PubMed GONUTS page
  2. 2.0 2.1 Tseng, MJ et al. (1992) Tandem cloning of bacteriophage T4 nrdA and nrdB genes and overproduction of ribonucleoside diphosphate reductase (alpha 2 beta 2) and a mutationally altered form (alpha 2 beta 2(93)). J. Bacteriol. 174 5740-4 PubMed GONUTS page
  3. Eriksson, M et al. (1997) Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure 5 1077-92 PubMed GONUTS page