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O15909

- RIR1_TRYBB

UniProt

O15909 - RIR1_TRYBB

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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RNR1

Organism
Trypanosoma brucei brucei
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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Allosteric activatorBy similarity
Binding sitei58 – 581Allosteric activatorBy similarity
Binding sitei93 – 931Allosteric activatorBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Sitei228 – 2281Important for hydrogen atom transferBy similarity
Sitei236 – 2361Allosteric effector binding, determines substrate specificityBy similarity
Binding sitei257 – 2571Substrate; via amide nitrogenBy similarity
Sitei266 – 2661Allosteric effector binding, determines substrate specificityBy similarity
Active sitei437 – 4371Proton acceptorBy similarity
Active sitei439 – 4391Cysteine radical intermediateBy similarity
Active sitei441 – 4411Proton acceptorBy similarity
Sitei454 – 4541Important for hydrogen atom transferBy similarity
Sitei759 – 7591Important for electron transferBy similarity
Sitei760 – 7601Important for electron transferBy similarity
Sitei833 – 8331Interacts with thioredoxin/glutaredoxinBy similarity
Sitei836 – 8361Interacts 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
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838Ribonucleoside-diphosphate reductase large subunitPRO_0000187199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi228 ↔ 454Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

3D structure databases

ProteinModelPortaliO15909.
SMRiO15909. Positions 23-777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 9792ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 227Allosteric activator bindingBy similarity
Regioni227 – 2282Substrate bindingBy similarity
Regioni295 – 2984Allosteric effector binding, determines substrate specificityBy similarity
Regioni437 – 4415Substrate bindingBy similarity
Regioni625 – 6295Substrate 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.

O15909-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLETVKLVTK RDGSVEPYDE KVVRSRIVNL MSGIDSYYVD VDDLVRVVGE
60 70 80 90 100
GVREGMSTSM LDELLAETAA YCVTKHPDYG LLAGRLAVTA LHKTTTESVL
110 120 130 140 150
DSFRVLHEHV SQATKRHAPL ISEELWDIAN KHSAALQQII NYERDFDFEY
160 170 180 190 200
FGYKTLERSY LLRVHKGRGV MEVVERPQQM FLRVALGIHG EDLERVKETY
210 220 230 240 250
DYMSQGFFTH ATPTLFNAGT PFPQMSSCFL VAMREDSIDG IYDTLKQCAI
260 270 280 290 300
ISKSAGGIGI HMHNIRAAGS YIAGTNGTSN GLVPMLRVWN NTARYVDQGG
310 320 330 340 350
GKRKGAFAIY LEPWHADIFG FLLLKKNTGK EDQRARDLFY GLWIPDLFME
360 370 380 390 400
RVESHGTWTL MDPNTAPFLS DCYGQEFTDL YERYEREGRG VRTIQAQELW
410 420 430 440 450
FLILESQVET GVPFMLYKDA CNFKSNQKNL GTIKCSNLCT EIVEYTSRDE
460 470 480 490 500
VAVCNLASIA LPRFVKDGAF DYVALKEVTK VVTRNLNRVI DRNHYPVCEA
510 520 530 540 550
RYSNLRHRPV GIGVQGLADA FALLSLPFAH PEAKKLNRQI FETIYIAAVE
560 570 580 590 600
ASTELAEKDG PYETFKGSPA SEGKLQFDLW DEERRIRGMN EDSVHSHCGL
610 620 630 640 650
WDWDSLKERV VKVGMRNSLL IAPMPTASTS QILGNNECIE PFTSNIYVRR
660 670 680 690 700
VLSGEFPVVN KHLVKELIRL RLWNDDMRRK IIALNGSVSG IKEIPERIRE
710 720 730 740 750
LYKVVWEIRQ KDLIDMAADR GRYIDQSQSL NLFLATPTSS QLTSMHFYSW
760 770 780 790 800
KKGLKTGMYY LRSQPAADAI KFTLDPKAMK ELPKPDKQSK EEVHGSVGRG
810 820 830
KRKRVGEKPT ANHSNAGAPN LNGPPDTDGD GGCLNCGS
Length:838
Mass (Da):94,619
Last modified:January 1, 1998 - v1
Checksum:i19A9B95525BAF69A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80910 mRNA. Translation: AAB70704.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80910 mRNA. Translation: AAB70704.1 .

3D structure databases

ProteinModelPortali O15909.
SMRi O15909. Positions 23-777.
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 and characterization of the R1 and R2 subunits of ribonucleotide reductase from Trypanosoma brucei."
    Hofer A., Schmidt P.P., Graslund A., Thelander L.
    Proc. Natl. Acad. Sci. U.S.A. 94:6959-6964(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 427.

Entry informationi

Entry nameiRIR1_TRYBB
AccessioniPrimary (citable) accession number: O15909
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 74 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