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

Q89AS4 (RIR1_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:bbp_168
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length761 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 – 761761Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187208

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
Site7541Interacts with thioredoxin/glutaredoxin By similarity
Site7591Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond225 ↔ 462Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AS4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7FB14E136283BDCF

FASTA76187,124
        10         20         30         40         50         60 
MNQMLFVTKR NGKIELINLD KIHRVLNWAA KGLENISISQ VALKSRIQFY NNIKTTIIHE 

        70         80         90        100        110        120 
TIIKAAADLI SENSPDYQYM AARLTIFHLR KKAFGQFNPP NLYDHVKNMI KLEKYDQHLL 

       130        140        150        160        170        180 
NDYPKQDFLI MNSFIKHRRD MNFSYAAVKQ LEGKYLIQNR VTKKIYESAQ FLYILISACL 

       190        200        210        220        230        240 
FSKYPNETRM KYIKNFYDAI STFKISLPTP IMAGLRTPTR QFSSCVLIES EDNLNSINAT 

       250        260        270        280        290        300 
TSAIVKYVSQ RAGIGINAGR IRALGSPIRN GDTLHTGCIP FYKHFQSAVK SCSQGGVRGG 

       310        320        330        340        350        360 
AATIFYPIWH FEIESLLVLK NNRGIEENRV RHMDYSVQLN KLMYQRLILG EHITLFSPSD 

       370        380        390        400        410        420 
VPNLYDSFFN NQEKFERLYI KYENDKTIRK KKVKASYLFS LMMQERTSTG RIYIQNVDHC 

       430        440        450        460        470        480 
NSHSAFNPKI APIRQSNLCL EITLPTKALQ DVHDKNGEIS LCTLSAINLG SLNNLNDLSK 

       490        500        510        520        530        540 
LSNLIVRALD SVLDYQEYPI LSAKKSALSR RTLGIGVINF AYYLAKNGVR YSDGSANNLT 

       550        560        570        580        590        600 
HRTFEAIQYH LLNASCVLAQ EKGACHWFSH TNYYKGILPI DTYKKNVDEI CNEPLHLDWE 

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

       670        680        690        700        710        720 
RLKNNYELLW NIPNNTGYLQ LASIMQKFVD QSISANTNYD PKLFPNNKIP MQQLILDLLT 

       730        740        750        760 
AYKLGLKTLY YQNTRDGASD HQTEDIQFSK NENCNHGACK I 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26901.1.
RefSeqNP_777796.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AS4.
SMRQ89AS4. Positions 5-737.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26901; AAO26901; bbp_168.
GeneID1058219.
KEGGbab:bbp168.
PATRIC21245113. VBIBucAph80364_0163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMALLWQMPS.
OrthoDBEOG6J48HC.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-168-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_BUCBP
AccessionPrimary (citable) accession number: Q89AS4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 82 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