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P50647

- RIR1_PLAFG

UniProt

P50647 - RIR1_PLAFG

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Protein
Ribonucleoside-diphosphate reductase large subunit
Gene
RNR1
Organism
Plasmodium falciparum (isolate FCR-3 / Gambia)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 sitei53 – 531Allosteric activator By similarity
Binding sitei88 – 881Allosteric activator By similarity
Binding sitei201 – 2011Substrate By similarity
Sitei217 – 2171Important for hydrogen atom transfer By similarity
Sitei225 – 2251Allosteric effector binding, determines substrate specificity By similarity
Binding sitei246 – 2461Substrate; via amide nitrogen By similarity
Sitei255 – 2551Allosteric 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
Sitei736 – 7361Important for electron transfer By similarity
Sitei737 – 7371Important for electron transfer By similarity
Sitei799 – 7991Interacts with thioredoxin/glutaredoxin By similarity
Sitei802 – 8021Interacts 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

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 FCR-3 / Gambia)
Taxonomic identifieri5838 [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 – 804804Ribonucleoside-diphosphate reductase large subunit
PRO_0000187197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi217 ↔ 442Redox-active By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

3D structure databases

ProteinModelPortaliP50647.
SMRiP50647. Positions 15-761.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-cone
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator binding By similarity
Regioni216 – 2172Substrate binding By similarity
Regioni284 – 2874Allosteric effector binding, determines substrate specificity By similarity
Regioni425 – 4295Substrate binding By similarity
Regioni602 – 6065Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

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.

P50647-1 [UniParc]FASTAAdd to Basket

« Hide

MYVLNRKGEE EDISFDQILK RIQRLSYGLH KLGEYPACVT QGVINGMYSS    50
IKTCELDELA AQTCAYMATT HPDFSILAAR ITTDNLHKNT SDDVAEVAEA 100
LYTYKDGRGR PASLISKEVY DFILLHKVRL NKEIDYTTHF NYDYFGFKTL 150
ERSYLLRINN KIIERPQHLL MRVSIGIHID DIDKALETYH LMSQKYFTHA 200
TPTLFNSGTP RPQMSSCFLL SMKADSIEGI FETLKQCALI SKTAGGIGVA 250
VQDIRGQNSY IRGTNGISNG LVPMLRVFND TARYVDQGGG KRKGSYAVYI 300
EPWHSDIFEF LDLRKNHGKE ELRARDLFYA VWVPDLFMKR VKENKNWTLM 350
CPNECPGLSE TWGEEFEKLY TKYEEENMGK KTVLAQDLWF AILQSQIETG 400
VPIYLYKDSC NAKPIKNLGT IKCSNLCCEI IEYTSPDEVA VCNLASIALC 450
KFVDLEKKEF NFKKLYEITK IITRNLDKII ERNYYPVKEA KTSNTRHRPI 500
GIGVQGLADT FMLLRYLYES DAAKELNKRI YETMYYAALE MSVDWLQSGP 550
YESYQGSPGS QGILQFDMWN AKVDNKYWDW DELKLKIAKT GLRNLLLLAP 600
MPTASTSQIL GNNESFEPYT SNIYYRRVLS GEFFVVNPHL LKDLFDRGLW 650
DEDMKQQLIA HNGSIQYISE IPDDLKELYK TVWEIKQKNI IDMAADRGYF 700
IDQSQSLNIY IQKPTFAKLS SMHFYGWEKG LKTGAYYLRT QAATDAIKFT 750
VDTHVAKNAV KLKNADGVQI TREVSRETIQ LNQRYSKCVS FKSNNDEQCL 800
MCSG 804
Length:804
Mass (Da):92,403
Last modified:October 1, 1996 - v1
Checksum:i8D3C70EA2ED0A6E9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF205580 Genomic DNA. Translation: AAA29755.1.
PIRiB48687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF205580 Genomic DNA. Translation: AAA29755.1 .
PIRi B48687.

3D structure databases

ProteinModelPortali P50647.
SMRi P50647. Positions 15-761.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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, sequence determination, and regulation of the ribonucleotide reductase subunits from Plasmodium falciparum: a target for antimalarial therapy."
    Rubin H., Salem J.S., Li L.S., Yang F.D., Mama S., Wang Z.M., Fisher A., Hamann C.S., Cooperman B.S.
    Proc. Natl. Acad. Sci. U.S.A. 90:9280-9284(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiRIR1_PLAFG
AccessioniPrimary (citable) accession number: P50647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 73 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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