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Q9ZLF9 (RIR1_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 101. 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:jhp_0621
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length788 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 – 788788Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187216

Regions

Domain2 – 9291ATP-cone
Region12 – 187Allosteric activator binding By similarity
Region215 – 2162Substrate binding By similarity
Region424 – 4285Substrate binding By similarity
Region659 – 6635Substrate binding By similarity

Sites

Active site4241Proton acceptor By similarity
Active site4261Cysteine radical intermediate By similarity
Active site4281Proton acceptor By similarity
Binding site61Allosteric activator By similarity
Binding site521Allosteric activator By similarity
Binding site2001Substrate By similarity
Binding site2441Substrate; via amide nitrogen By similarity
Site2161Important for hydrogen atom transfer By similarity
Site2231Allosteric effector binding By similarity
Site2531Allosteric effector binding By similarity
Site4971Important for hydrogen atom transfer By similarity
Site7631Important for electron transfer By similarity
Site7641Important for electron transfer By similarity
Site7841Interacts with thioredoxin/glutaredoxin By similarity
Site7871Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond216 ↔ 497Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZLF9 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A98AFCBC5CC6398E

FASTA78890,232
        10         20         30         40         50         60 
MITVVKRNGR IEPLDITKIQ KYTKDATDNL EGVSQSELEV DARLQFRDKI TTEEIQQTLI 

        70         80         90        100        110        120 
KTAVDKIDID TPNWSFVASR LFLYDLYHKV SGFTGYRHLK EYFENAEEKG RILKGFKEKF 

       130        140        150        160        170        180 
DLEFLNSQIK PERDFQFNYL GIKTLYDRYL LKDANNHPIE LPQHMFMSIA MFLAQNEQEL 

       190        200        210        220        230        240 
NKIALEFYEV LSKFEAMCAT PTLANARTTK HQLSSCYIGS TPDNIEGIFD SYKEMALLSK 

       250        260        270        280        290        300 
YGGGIGWDFS LVRSIGSYID GHKNASAGTI PFLKIANDVA IAVDQLGTRK GAIAVYLEIW 

       310        320        330        340        350        360 
HIDVMEFIDL RKNSGDERRR AHDLFPALWV CDLFMKRVLE DAMWTLFDPY ECKDLTELYG 

       370        380        390        400        410        420 
QDFEKRYLEY EKDPKIIKEY INAKDLWKKI LMNYFEAGLP FLAFKDNANR CNPNAHAGII 

       430        440        450        460        470        480 
RSSNLCTEIF QNTAPNHYYM QIEYTDGAIE FFEEKELVTT DSNITKCANK LTSTDILKGK 

       490        500        510        520        530        540 
KIYIATKVAK DGQTAVCNLA SINLSKINTE EDIKRVVPIM VRLLDNVIDL NFYPNRKVKA 

       550        560        570        580        590        600 
TNLQNRAIGL GVMGEAQMLA EHQIAWGSKE HLEKIDALME QISYHAIDTS ANLAKEKGVY 

       610        620        630        640        650        660 
KDFENSEWSK GIFPIDKANN EALKLTEKGL FNHACDWQGL REKVKANGMR NGYLMAIAPT 

       670        680        690        700        710        720 
SSISILVGTT QTIEPIYKKK WFEENLSGLI PVVVPNLNVE TWNFYTSAYD IDAKDLIKAA 

       730        740        750        760        770        780 
AVRQKWIDQG QSINVFLRIE NASGKTLHEI YTLAWKLGLK STYYLRSESP SIDEKSVLDR 


SVECFNCQ 

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References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06201.1.
PIRF71908.
RefSeqNP_223339.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZLF9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp0621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06201; AAD06201; jhp_0621.
GeneID890291.
KEGGhpj:jhp0621.
PATRIC20605953. VBIHelPyl98156_0682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMADLNFYPN.
OrthoDBEOG6J48HC.
ProtClustDBPRK08447.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-632-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZLF9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 13, 2013
This is version 101 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