Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O66503 (RIR1_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 100. 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 subunit alpha

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase
Gene names
Name:nrdA
Ordered Locus Names:aq_094
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length801 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 By similarity.

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 alpha 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

Tetramer of two alpha and two beta subunits By similarity.

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 – 801801Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187205

Regions

Domain3 – 9290ATP-cone
Region13 – 197Allosteric activator binding By similarity
Region234 – 2352Substrate binding By similarity
Region483 – 4875Substrate binding By similarity
Region680 – 6845Substrate binding By similarity

Sites

Active site4831Proton acceptor By similarity
Active site4851Cysteine radical intermediate By similarity
Active site4871Proton acceptor By similarity
Binding site71Allosteric activator By similarity
Binding site521Allosteric activator By similarity
Binding site881Allosteric activator By similarity
Binding site2191Substrate By similarity
Binding site2631Substrate; via amide nitrogen By similarity
Site2351Important for hydrogen atom transfer By similarity
Site2421Allosteric effector binding By similarity
Site2721Allosteric effector binding By similarity
Site5211Important for hydrogen atom transfer By similarity
Site7831Important for electron transfer By similarity
Site7841Important for electron transfer By similarity
Site7961Interacts with thioredoxin/glutaredoxin By similarity
Site7991Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond235 ↔ 521Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O66503 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: FF728EDC7D97C396

FASTA80192,914
        10         20         30         40         50         60 
MTMYVIKRSG RKEKLDINKI RIAIKFACEG LNVDPLELEA DAQIQFRDGI TTKEIQQLLI 

        70         80         90        100        110        120 
KTAAEKVSAE RPDWTYTAAR LLLYDLYKDV AHLRGYSLRD DLGKYKPYNR KNFYSFVKEY 

       130        140        150        160        170        180 
VEKGIYGEYL LENYSEEDFN KLANYIKPER DLYFTYTGIK ILYDRYLVRD EEGRVIELPQ 

       190        200        210        220        230        240 
EMYMLIAMTL AVPEKPEERL KWAKKFYDVL SEHKVTVATP TLMNARRPFT QLSSCFVLTV 

       250        260        270        280        290        300 
DDDLFDIFDN VKKAGMISKF AGGLGVYLGK IRATGAPIRK FKGASSGVIP VVKLINDTMT 

       310        320        330        340        350        360 
YVDQLGMRKG SASITLDIWH KDILDFLEVK TNVGDERKKA HDIHPAVSIP DLFMKRLKNR 

       370        380        390        400        410        420 
EDWTLIDPYW ARQYITRKIY DGKYKEVKPL PGSHYYVGIK EDGTQDILEP KGLEDFYGEE 

       430        440        450        460        470        480 
FEKWYLELEE NLPSYAKKKV NSFELWKRLL TVAFETGEPY IFFRDEANRK NPNKHTGMVY 

       490        500        510        520        530        540 
SSNLCHEIVQ TMSPSKHEKP VLDPETGEIT YKKEAGDLPV CNLGSVNLGK VHTEEEIKEV 

       550        560        570        580        590        600 
LPLLVRMLDN VIEMNFYAIP EAEYTNKRYR AIGIGVSNYH YCLVKNGIKW ESEEHLKFAD 

       610        620        630        640        650        660 
KLFELIAFYA LKGSLELAKE RGRYKLFDGS NWSKGILFGR SVEEIEENSR QNGNNLPWRE 

       670        680        690        700        710        720 
LAEEIKKYGI RNAYLLALMP TGSTSLILGA TPSIDPIFAR FYKEENMSGI LPQVPPEVDR 

       730        740        750        760        770        780 
FYWHYKTAYT IDHEWTIRAA AVRQKWIDQA QSLNLFVDPQ NIDGPRLSRL YELAWELGLK 

       790        800 
TIYYLRSRSA MDIEECEACS V 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06460.1.
PIRD70309.
RefSeqNP_213062.1. NC_000918.1.

3D structure databases

ProteinModelPortalO66503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC06460; AAC06460; aq_094.
GeneID1192514.
KEGGaae:aq_094.
PATRIC20957884. VBIAquAeo85532_0082.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057034.
KOK00525.
OMAEIMLHTG.
OrthoDBEOG6J48HC.
ProtClustDBCLSK2748242.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-77-MONOMER.
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_AQUAE
AccessionPrimary (citable) accession number: O66503
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways