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P50648

- RIR1_PLAF4

UniProt

P50648 - RIR1_PLAF4

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Protein
Ribonucleoside-diphosphate reductase large subunit
Gene
RNR1
Organism
Plasmodium falciparum (isolate Dd2)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521Allosteric activator By similarity
Binding sitei87 – 871Allosteric activator By similarity
Binding sitei200 – 2001Substrate By similarity
Sitei216 – 2161Important for hydrogen atom transfer By similarity
Sitei224 – 2241Allosteric effector binding, determines substrate specificity By similarity
Binding sitei245 – 2451Substrate; via amide nitrogen By similarity
Sitei254 – 2541Allosteric effector binding, determines substrate specificity By similarity
Active sitei425 – 4251Proton acceptor By similarity
Active sitei427 – 4271Cysteine radical intermediate By similarity
Active sitei429 – 4291Proton acceptor By similarity
Sitei442 – 4421Important for hydrogen atom transfer By similarity
Sitei737 – 7371Important for electron transfer By similarity
Sitei738 – 7381Important for electron transfer By similarity
Sitei801 – 8011Interacts with thioredoxin/glutaredoxin By similarity
Sitei804 – 8041Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. deoxyribonucleotide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase R1 subunit
Gene namesi
Name:RNR1
OrganismiPlasmodium falciparum (isolate Dd2)
Taxonomic identifieri57267 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 806806Ribonucleoside-diphosphate reductase large subunit
PRO_0000187198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi216 ↔ 442Redox-active By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

3D structure databases

ProteinModelPortaliP50648.
SMRiP50648. Positions 15-762.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191ATP-cone
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator binding By similarity
Regioni215 – 2162Substrate binding By similarity
Regioni283 – 2864Allosteric effector binding, determines substrate specificity By similarity
Regioni425 – 4295Substrate binding By similarity
Regioni603 – 6075Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Phylogenomic databases

eggNOGiCOG0209.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50648-1 [UniParc]FASTAAdd to Basket

« Hide

MYVLNRKGEE EDISFDQILK RIQRLSYGLH ELVDPARVTQ GVINGMYSGI    50
KTCELDELAA QTCAYMATTH PDFSILAARI TTDNLHKNTS DDVAEVAEAL 100
YTYKDVRGRP ASLISKEVYD FILLHKDRLN KEIDYTRDFN YDYFGFKTLE 150
RSYLLRINNK IIERPQHLLM RVSIGIHIDD IDKALETYHL MSQKYFTHAT 200
PTLFNSGTPR PQMSSCFLLS MKADSIEGIF ETLKQCALIS KTAGGIGVAV 250
QDIRGQNSYI RGTNGISNGL VPMLRVFNDT ARYVDQGGGK RKGSFAVYIE 300
PWHSDIFEFL DLRKNHGKEE LRARDLFYAV WVPDLFMKRV KENKNWTLMC 350
PNECPGLSET WGEEFEKLYT KYEEENMGKK TVLAQDLWFA ILQSQIETGV 400
PYMLYKDSCN AKSNQKNLGT IKCSNLCCEI IEYTSPDEVA VCNLASIALC 450
KFVDLEKKEF NFKKLYEITK IITRNLDKII ERNYYPVKEA KTSNTRHRPI 500
GIGVQGLADT FMLLRYPYES DAAKELNKRI FETMYYAALE MSVELASIHG 550
PYESYQGSPA SQGILQFDMW NAKVDNKYWD WDELKAKIRK HGLRNSLLLA 600
PMPTASTSQI LGNNESFEPY TSNIYYRRVL SGEFFVVNPH LLKDLFDRGL 650
WDEDMKQQLI AHNGSIQYIS EIPDDLKELY KTVWEIKQKN IIDMAADRGI 700
FIDQSQSLNI YIQKPTFAKL SSMHFYGWEK GLKTGAYYLR TQAATDAIKF 750
TVDTHVAKNA VKLKNADGVQ ITREVSRETI STESTVTQNV CPLRRNNDEQ 800
CLMCSG 806
Length:806
Mass (Da):92,513
Last modified:October 1, 1996 - v1
Checksum:iA23B414A687B275F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01323 mRNA. Translation: AAA50171.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01323 mRNA. Translation: AAA50171.1 .

3D structure databases

ProteinModelPortali P50648.
SMRi P50648. Positions 15-762.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0209.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiRIR1_PLAF4
AccessioniPrimary (citable) accession number: P50648
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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