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P50647 (RIR1_PLAFG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. 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 FCR-3 / Gambia)
Taxonomic identifier5838 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length804 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 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 – 804804Ribonucleoside-diphosphate reductase large subunit
PRO_0000187197

Regions

Domain1 – 9292ATP-cone
Region11 – 177Allosteric activator binding By similarity
Region216 – 2172Substrate binding By similarity
Region284 – 2874Allosteric effector binding, determines substrate specificity By similarity
Region425 – 4295Substrate binding By similarity
Region602 – 6065Substrate binding By similarity

Sites

Active site4251Proton acceptor By similarity
Active site4271Cysteine radical intermediate By similarity
Active site4291Proton acceptor By similarity
Binding site531Allosteric activator By similarity
Binding site881Allosteric activator By similarity
Binding site2011Substrate By similarity
Binding site2461Substrate; via amide nitrogen By similarity
Site2171Important for hydrogen atom transfer By similarity
Site2251Allosteric effector binding, determines substrate specificity By similarity
Site2551Allosteric effector binding, determines substrate specificity By similarity
Site4421Important for hydrogen atom transfer By similarity
Site7361Important for electron transfer By similarity
Site7371Important for electron transfer By similarity
Site7991Interacts with thioredoxin/glutaredoxin By similarity
Site8021Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond217 ↔ 442Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P50647 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8D3C70EA2ED0A6E9

FASTA80492,403
        10         20         30         40         50         60 
MYVLNRKGEE EDISFDQILK RIQRLSYGLH KLGEYPACVT QGVINGMYSS IKTCELDELA 

        70         80         90        100        110        120 
AQTCAYMATT HPDFSILAAR ITTDNLHKNT SDDVAEVAEA LYTYKDGRGR PASLISKEVY 

       130        140        150        160        170        180 
DFILLHKVRL NKEIDYTTHF NYDYFGFKTL ERSYLLRINN KIIERPQHLL MRVSIGIHID 

       190        200        210        220        230        240 
DIDKALETYH LMSQKYFTHA TPTLFNSGTP RPQMSSCFLL SMKADSIEGI FETLKQCALI 

       250        260        270        280        290        300 
SKTAGGIGVA VQDIRGQNSY IRGTNGISNG LVPMLRVFND TARYVDQGGG KRKGSYAVYI 

       310        320        330        340        350        360 
EPWHSDIFEF LDLRKNHGKE ELRARDLFYA VWVPDLFMKR VKENKNWTLM CPNECPGLSE 

       370        380        390        400        410        420 
TWGEEFEKLY TKYEEENMGK KTVLAQDLWF AILQSQIETG VPIYLYKDSC NAKPIKNLGT 

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

       490        500        510        520        530        540 
ERNYYPVKEA KTSNTRHRPI GIGVQGLADT FMLLRYLYES DAAKELNKRI YETMYYAALE 

       550        560        570        580        590        600 
MSVDWLQSGP YESYQGSPGS QGILQFDMWN AKVDNKYWDW DELKLKIAKT GLRNLLLLAP 

       610        620        630        640        650        660 
MPTASTSQIL GNNESFEPYT SNIYYRRVLS GEFFVVNPHL LKDLFDRGLW DEDMKQQLIA 

       670        680        690        700        710        720 
HNGSIQYISE IPDDLKELYK TVWEIKQKNI IDMAADRGYF IDQSQSLNIY IQKPTFAKLS 

       730        740        750        760        770        780 
SMHFYGWEKG LKTGAYYLRT QAATDAIKFT VDTHVAKNAV KLKNADGVQI TREVSRETIQ 

       790        800 
LNQRYSKCVS FKSNNDEQCL MCSG 

« Hide

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF205580 Genomic DNA. Translation: AAA29755.1.
PIRB48687.

3D structure databases

ProteinModelPortalP50647.
SMRP50647. Positions 15-761.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PLAFG
AccessionPrimary (citable) accession number: P50647
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways