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O15909 (RIR1_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. 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
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 – 838838Ribonucleoside-diphosphate reductase large subunit
PRO_0000187199

Regions

Domain6 – 9792ATP-cone
Region16 – 227Allosteric activator binding By similarity
Region227 – 2282Substrate binding By similarity
Region295 – 2984Allosteric effector binding, determines substrate specificity By similarity
Region437 – 4415Substrate binding By similarity
Region625 – 6295Substrate binding By similarity

Sites

Active site4371Proton acceptor By similarity
Active site4391Cysteine radical intermediate By similarity
Active site4411Proton acceptor By similarity
Binding site101Allosteric activator By similarity
Binding site581Allosteric activator By similarity
Binding site931Allosteric activator By similarity
Binding site2121Substrate By similarity
Binding site2571Substrate; via amide nitrogen By similarity
Site2281Important for hydrogen atom transfer By similarity
Site2361Allosteric effector binding, determines substrate specificity By similarity
Site2661Allosteric effector binding, determines substrate specificity By similarity
Site4541Important for hydrogen atom transfer By similarity
Site7591Important for electron transfer By similarity
Site7601Important for electron transfer By similarity
Site8331Interacts with thioredoxin/glutaredoxin By similarity
Site8361Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond228 ↔ 454Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O15909 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 19A9B95525BAF69A

FASTA83894,619
        10         20         30         40         50         60 
MLETVKLVTK RDGSVEPYDE KVVRSRIVNL MSGIDSYYVD VDDLVRVVGE GVREGMSTSM 

        70         80         90        100        110        120 
LDELLAETAA YCVTKHPDYG LLAGRLAVTA LHKTTTESVL DSFRVLHEHV SQATKRHAPL 

       130        140        150        160        170        180 
ISEELWDIAN KHSAALQQII NYERDFDFEY FGYKTLERSY LLRVHKGRGV MEVVERPQQM 

       190        200        210        220        230        240 
FLRVALGIHG EDLERVKETY DYMSQGFFTH ATPTLFNAGT PFPQMSSCFL VAMREDSIDG 

       250        260        270        280        290        300 
IYDTLKQCAI ISKSAGGIGI HMHNIRAAGS YIAGTNGTSN GLVPMLRVWN NTARYVDQGG 

       310        320        330        340        350        360 
GKRKGAFAIY LEPWHADIFG FLLLKKNTGK EDQRARDLFY GLWIPDLFME RVESHGTWTL 

       370        380        390        400        410        420 
MDPNTAPFLS DCYGQEFTDL YERYEREGRG VRTIQAQELW FLILESQVET GVPFMLYKDA 

       430        440        450        460        470        480 
CNFKSNQKNL GTIKCSNLCT EIVEYTSRDE VAVCNLASIA LPRFVKDGAF DYVALKEVTK 

       490        500        510        520        530        540 
VVTRNLNRVI DRNHYPVCEA RYSNLRHRPV GIGVQGLADA FALLSLPFAH PEAKKLNRQI 

       550        560        570        580        590        600 
FETIYIAAVE ASTELAEKDG PYETFKGSPA SEGKLQFDLW DEERRIRGMN EDSVHSHCGL 

       610        620        630        640        650        660 
WDWDSLKERV VKVGMRNSLL IAPMPTASTS QILGNNECIE PFTSNIYVRR VLSGEFPVVN 

       670        680        690        700        710        720 
KHLVKELIRL RLWNDDMRRK IIALNGSVSG IKEIPERIRE LYKVVWEIRQ KDLIDMAADR 

       730        740        750        760        770        780 
GRYIDQSQSL NLFLATPTSS QLTSMHFYSW KKGLKTGMYY LRSQPAADAI KFTLDPKAMK 

       790        800        810        820        830 
ELPKPDKQSK EEVHGSVGRG KRKRVGEKPT ANHSNAGAPN LNGPPDTDGD GGCLNCGS 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U80910 mRNA. Translation: AAB70704.1.

3D structure databases

ProteinModelPortalO15909.
SMRO15909. Positions 23-777.
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_TRYBB
AccessionPrimary (citable) accession number: O15909
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 72 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