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Q8K9W3 (RIR1_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_173
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length763 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 763763Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187207

Regions

Domain5 – 9591ATP-cone
Region15 – 217Allosteric activator binding By similarity
Region224 – 2252Substrate binding By similarity
Region437 – 4415Substrate binding By similarity
Region621 – 6255Substrate binding By similarity

Sites

Active site4371Proton acceptor By similarity
Active site4391Cysteine radical intermediate By similarity
Active site4411Proton acceptor By similarity
Binding site91Allosteric activator By similarity
Binding site551Allosteric activator By similarity
Binding site911Allosteric activator By similarity
Binding site2091Substrate By similarity
Binding site2531Substrate; via amide nitrogen By similarity
Site2251Important for hydrogen atom transfer By similarity
Site2321Allosteric effector binding By similarity
Site2621Allosteric effector binding By similarity
Site4621Important for hydrogen atom transfer By similarity
Site7301Important for electron transfer By similarity
Site7311Important for electron transfer By similarity
Site7561Interacts with thioredoxin/glutaredoxin By similarity
Site7611Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond225 ↔ 462Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9W3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: BDE02289A8CF8D3D

FASTA76387,471
        10         20         30         40         50         60 
MKNSLFVTKR NGKKEKINLD KIHKVLNWAA KGLENISVSQ VELRSRIQFY NNISTVNIHE 

        70         80         90        100        110        120 
TIIKAAADLI SENTPDYQYM AARLAIFHLR KKAYGQFEPP NLYYHVKKMV QLGKYDEKLL 

       130        140        150        160        170        180 
QNYSFEEYVE MNSFVDHRRD MNFSYAAVKQ LEAKYLLQNR VTGQIYESAQ FLYILISACL 

       190        200        210        220        230        240 
FSKYEKKVRM NYIQRFYNAI STFKISLPTP IMSGVRTPTR QFSSCVLIEC ADNLNSINAT 

       250        260        270        280        290        300 
TSAIVKYVSQ RAGIGINAGQ IRALGSPIRN GEAFHTGCIP FYKHFQSAVK SCSQGGVRGG 

       310        320        330        340        350        360 
AATVFYPIWH LEIESLLVLK NNRGIEENRV RHLDYAVQIN KLMYQRMLLG QKITLFSPSD 

       370        380        390        400        410        420 
VPKLYEFFFS DQKKFKEIYI KYEKNRNIRK KSINAIDLFC LIMRERASTG RIYIQHVDHC 

       430        440        450        460        470        480 
NSHSAFNSKL ATIRQSNLCL EITLPTKPLN NIDDKNGEIA LCTLSALNLG LINDLHDLKE 

       490        500        510        520        530        540 
LSTLSVRALD EILEYQNYPV VCAKKSAISR RSLGIGVINF AYYLAKNKVR YSDGSAKNLT 

       550        560        570        580        590        600 
HKTFEAIQYY LLKASCELAK EKGSCSLFNQ TNYYLGKFPI DTYKKDIDSI CNEPLHLNWN 

       610        620        630        640        650        660 
LLRKKIKKYG LRNSTLSALM PSETSSQISN ATNGIEPPRG FISIKSSKDG MLRQVVPEYK 

       670        680        690        700        710        720 
KLKSEYELLW EIPNNIGYLE LVAIMQKFVD QSISANTNYD PKRFLNEKIP MKQLIYDLLV 

       730        740        750        760 
AYKLGIKTLY YQNTRDGAED NQNLNKSIEN IKEDNCTSGS CTI 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67739.1.
RefSeqNP_660528.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9W3.
SMRQ8K9W3. Positions 5-737.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg173.

Proteomic databases

PRIDEQ8K9W3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67739; AAM67739; BUsg_173.
GeneID1005370.
KEGGbas:BUsg173.
PATRIC21247127. VBIBucAph100086_0177.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMALLWQMPS.
OrthoDBEOG6J48HC.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-182-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_BUCAP
AccessionPrimary (citable) accession number: Q8K9W3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 90 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names