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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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Allosteric activatorBy similarity
Binding sitei88 – 881Allosteric activatorBy similarity
Binding sitei201 – 2011SubstrateBy similarity
Sitei217 – 2171Important for hydrogen atom transferBy similarity
Sitei225 – 2251Allosteric effector binding, determines substrate specificityBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
Sitei255 – 2551Allosteric effector binding, determines substrate specificityBy similarity
Active sitei425 – 4251Proton acceptorBy similarity
Active sitei427 – 4271Cysteine radical intermediateBy similarity
Active sitei429 – 4291Proton acceptorBy similarity
Sitei442 – 4421Important for hydrogen atom transferBy similarity
Sitei736 – 7361Important for electron transferBy similarity
Sitei737 – 7371Important for electron transferBy similarity
Sitei799 – 7991Interacts with thioredoxin/glutaredoxinBy similarity
Sitei802 – 8021Interacts with thioredoxin/glutaredoxinBy 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. deoxyribonucleotide biosynthetic process Source: UniProtKB
  2. DNA replication Source: UniProtKB-UniPathway
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)

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 804804Ribonucleoside-diphosphate reductase large subunitPRO_0000187197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi217 ↔ 442Redox-activeBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MYVLNRKGEE EDISFDQILK RIQRLSYGLH KLGEYPACVT QGVINGMYSS
60 70 80 90 100
IKTCELDELA AQTCAYMATT HPDFSILAAR ITTDNLHKNT SDDVAEVAEA
110 120 130 140 150
LYTYKDGRGR PASLISKEVY DFILLHKVRL NKEIDYTTHF NYDYFGFKTL
160 170 180 190 200
ERSYLLRINN KIIERPQHLL MRVSIGIHID DIDKALETYH LMSQKYFTHA
210 220 230 240 250
TPTLFNSGTP RPQMSSCFLL SMKADSIEGI FETLKQCALI SKTAGGIGVA
260 270 280 290 300
VQDIRGQNSY IRGTNGISNG LVPMLRVFND TARYVDQGGG KRKGSYAVYI
310 320 330 340 350
EPWHSDIFEF LDLRKNHGKE ELRARDLFYA VWVPDLFMKR VKENKNWTLM
360 370 380 390 400
CPNECPGLSE TWGEEFEKLY TKYEEENMGK KTVLAQDLWF AILQSQIETG
410 420 430 440 450
VPIYLYKDSC NAKPIKNLGT IKCSNLCCEI IEYTSPDEVA VCNLASIALC
460 470 480 490 500
KFVDLEKKEF NFKKLYEITK IITRNLDKII ERNYYPVKEA KTSNTRHRPI
510 520 530 540 550
GIGVQGLADT FMLLRYLYES DAAKELNKRI YETMYYAALE MSVDWLQSGP
560 570 580 590 600
YESYQGSPGS QGILQFDMWN AKVDNKYWDW DELKLKIAKT GLRNLLLLAP
610 620 630 640 650
MPTASTSQIL GNNESFEPYT SNIYYRRVLS GEFFVVNPHL LKDLFDRGLW
660 670 680 690 700
DEDMKQQLIA HNGSIQYISE IPDDLKELYK TVWEIKQKNI IDMAADRGYF
710 720 730 740 750
IDQSQSLNIY IQKPTFAKLS SMHFYGWEKG LKTGAYYLRT QAATDAIKFT
760 770 780 790 800
VDTHVAKNAV KLKNADGVQI TREVSRETIQ LNQRYSKCVS FKSNNDEQCL

MCSG
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 29, 2014
This is version 75 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