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P32282 (RIR1_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase subunit alpha

EC=1.17.4.1
Alternative name(s):
Protein B1
Ribonucleotide reductase
Gene names
Name:NRDA
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length754 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulation

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterodimer of a large and a small subunit.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 1 ATP-cone domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 754754Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187226

Regions

Domain4 – 9390ATP-cone
Region221 – 2222Substrate binding By similarity
Region435 – 4395Substrate binding By similarity
Region615 – 6195Substrate binding By similarity

Sites

Active site4351Proton acceptor By similarity
Active site4371Cysteine radical intermediate By similarity
Active site4391Proton acceptor By similarity
Binding site2061Substrate By similarity
Binding site2501Substrate; via amide nitrogen By similarity
Site2221Important for hydrogen atom transfer By similarity
Site2291Allosteric effector binding By similarity
Site2591Allosteric effector binding By similarity
Site4571Important for hydrogen atom transfer By similarity
Site7261Important for electron transfer By similarity
Site7271Important for electron transfer By similarity
Site7491Interacts with thioredoxin/glutaredoxin By similarity
Site7521Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond222 ↔ 457Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P32282 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 31D178EAA580068A

FASTA75485,973
        10         20         30         40         50         60 
MQLINVIKSS GVSQSFDPQK IIKVLSWAAE GTSVDPYELY ENIKSYLRDG MTTDDIQTIV 

        70         80         90        100        110        120 
IKAAANSISV EEPDYQYVAA RCLMFALRKH VYGQYEPRSF IDHISYCVNA GKYDPELLSK 

       130        140        150        160        170        180 
YSAEEITFLE SKIKHERDME FTYSGAMQLK EKYLVKDKTT GQIYETPQFA FMTIGMALHQ 

       190        200        210        220        230        240 
DEPVDRLKHV IRFYEAVSTR QISLPTPIMA GCRTPTRQFS SCVVIEAGDS LKSINKASAS 

       250        260        270        280        290        300 
IVEYISKRAG IGINVGMIRA EGSKIGMGEV RHTGVIPFWK HFQTAVKSCS QGGIRGGAAT 

       310        320        330        340        350        360 
AYYPIWHLEV ENLLVLKNNK GVEENRIRHM DYGVQLNDLM MERFGKNDYI TLFSPHEMGG 

       370        380        390        400        410        420 
ELYYSYFKDQ DRFRELYEAA EKDPNIRKKR IKARELFELL MTERSGTARI YVQFIDNTNN 

       430        440        450        460        470        480 
YTPFIREKAP IRQSNLCCEI AIPTNDVNSP DAEIGLCTLS AFVLDNFDWQ DQDKINELAE 

       490        500        510        520        530        540 
VQVRALDNLL DYQGYPVPEA EKAKKRRNLG VGVTNYAAWL ASNFASYEDA NDLTHELFER 

       550        560        570        580        590        600 
LQYGLIKASI KLAKEKGPSE YYSDTRWSRG ELPIDWYNKK IDQIAAPKYV CDWSALREDL 

       610        620        630        640        650        660 
KLFGIRNSTL SALMPCESSS QVSNSTNGYE PPRGPVSVKE SKEGSFNQVV PNIEHNIDLY 

       670        680        690        700        710        720 
DYTWKLAKKG NKPYLTQVAI MLKWVCQSAS ANTYYDPQIF PKGKVPMSIM IDDMLYGWYY 

       730        740        750 
GIKNFYYHNT RDGSGTDDYE IETPKADDCA ACKL 

« Hide

References

« Hide 'large scale' references
[1]"Total sequence, flanking regions, and transcripts of bacteriophage T4 nrdA gene, coding for alpha chain of ribonucleoside diphosphate reductase."
Tseng M.J., Hilfinger J.M., Walsh A., Greenberg G.R.
J. Biol. Chem. 263:16242-16251(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Localization of the T4 phage ribonucleotide reductase B1 subunit gene and the nucleotide sequence of its upstream and 5' coding regions."
Chu F.K., Maley G.F., Wang A.M., Maley F.
Gene 57:143-148(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03968 Genomic DNA. Translation: AAA32527.1.
AF158101 Genomic DNA. Translation: AAD42621.1.
M22627 Genomic DNA. Translation: AAA32531.1.
RefSeqNP_049845.1. NC_000866.4.

3D structure databases

ProteinModelPortalP32282.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258795.

Phylogenomic databases

ProtClustDBPHA2572.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_BPT4
AccessionPrimary (citable) accession number: P32282
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 16, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways