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P50648 (RIR1_PLAF4) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. 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 large subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase R1 subunit
Gene names
Name:RNR1
OrganismPlasmodium falciparum (isolate Dd2)
Taxonomic identifier57267 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 to separate specificity and activation sites on the large subunit. 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. Stimulated by ATP and inhibited by dATP binding to the activity site 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 – 806806Ribonucleoside-diphosphate reductase large subunit
PRO_0000187198

Regions

Domain1 – 9191ATP-cone
Region11 – 177Allosteric activator binding By similarity
Region215 – 2162Substrate binding By similarity
Region283 – 2864Allosteric effector binding, determines substrate specificity By similarity
Region425 – 4295Substrate binding By similarity
Region603 – 6075Substrate binding By similarity

Sites

Active site4251Proton acceptor By similarity
Active site4271Cysteine radical intermediate By similarity
Active site4291Proton acceptor By similarity
Binding site521Allosteric activator By similarity
Binding site871Allosteric activator By similarity
Binding site2001Substrate By similarity
Binding site2451Substrate; via amide nitrogen By similarity
Site2161Important for hydrogen atom transfer By similarity
Site2241Allosteric effector binding, determines substrate specificity By similarity
Site2541Allosteric effector binding, determines substrate specificity By similarity
Site4421Important for hydrogen atom transfer By similarity
Site7371Important for electron transfer By similarity
Site7381Important for electron transfer By similarity
Site8011Interacts with thioredoxin/glutaredoxin By similarity
Site8041Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond216 ↔ 442Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P50648 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A23B414A687B275F

FASTA80692,513
        10         20         30         40         50         60 
MYVLNRKGEE EDISFDQILK RIQRLSYGLH ELVDPARVTQ GVINGMYSGI KTCELDELAA 

        70         80         90        100        110        120 
QTCAYMATTH PDFSILAARI TTDNLHKNTS DDVAEVAEAL YTYKDVRGRP ASLISKEVYD 

       130        140        150        160        170        180 
FILLHKDRLN KEIDYTRDFN YDYFGFKTLE RSYLLRINNK IIERPQHLLM RVSIGIHIDD 

       190        200        210        220        230        240 
IDKALETYHL MSQKYFTHAT PTLFNSGTPR PQMSSCFLLS MKADSIEGIF ETLKQCALIS 

       250        260        270        280        290        300 
KTAGGIGVAV QDIRGQNSYI RGTNGISNGL VPMLRVFNDT ARYVDQGGGK RKGSFAVYIE 

       310        320        330        340        350        360 
PWHSDIFEFL DLRKNHGKEE LRARDLFYAV WVPDLFMKRV KENKNWTLMC PNECPGLSET 

       370        380        390        400        410        420 
WGEEFEKLYT KYEEENMGKK TVLAQDLWFA ILQSQIETGV PYMLYKDSCN AKSNQKNLGT 

       430        440        450        460        470        480 
IKCSNLCCEI IEYTSPDEVA VCNLASIALC KFVDLEKKEF NFKKLYEITK IITRNLDKII 

       490        500        510        520        530        540 
ERNYYPVKEA KTSNTRHRPI GIGVQGLADT FMLLRYPYES DAAKELNKRI FETMYYAALE 

       550        560        570        580        590        600 
MSVELASIHG PYESYQGSPA SQGILQFDMW NAKVDNKYWD WDELKAKIRK HGLRNSLLLA 

       610        620        630        640        650        660 
PMPTASTSQI LGNNESFEPY TSNIYYRRVL SGEFFVVNPH LLKDLFDRGL WDEDMKQQLI 

       670        680        690        700        710        720 
AHNGSIQYIS EIPDDLKELY KTVWEIKQKN IIDMAADRGI FIDQSQSLNI YIQKPTFAKL 

       730        740        750        760        770        780 
SSMHFYGWEK GLKTGAYYLR TQAATDAIKF TVDTHVAKNA VKLKNADGVQ ITREVSRETI 

       790        800 
STESTVTQNV CPLRRNNDEQ CLMCSG 

« Hide

References

[1]"Cloning and characterization of subunit genes of ribonucleotide reductase, a cell-cycle-regulated enzyme, from Plasmodium falciparum."
Chakrabarti D., Schuster S.M., Chakrabarti R.
Proc. Natl. Acad. Sci. U.S.A. 90:12020-12024(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01323 mRNA. Translation: AAA50171.1.

3D structure databases

ProteinModelPortalP50648.
SMRP50648. Positions 15-762.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0209.

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_PLAF4
AccessionPrimary (citable) accession number: P50648
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways