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

P50620 (RIR1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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 large subunit
Gene names
Name:nrdE
Synonyms:nrdA
Ordered Locus Names:BSU17380
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length700 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. 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 700700Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187209

Regions

Region169 – 1702Substrate binding By similarity
Region380 – 3845Substrate binding By similarity
Region580 – 5845Substrate binding By similarity

Sites

Active site3801Proton acceptor By similarity
Active site3821Cysteine radical intermediate By similarity
Active site3841Proton acceptor By similarity
Binding site1531Substrate By similarity
Binding site1981Substrate; via amide nitrogen By similarity
Site1701Important for hydrogen atom transfer By similarity
Site1771Allosteric effector binding By similarity
Site2071Allosteric effector binding By similarity
Site4091Important for hydrogen atom transfer By similarity
Site6831Important for electron transfer By similarity
Site6841Important for electron transfer By similarity
Site6951Interacts with thioredoxin/glutaredoxin By similarity
Site6981Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond170 ↔ 409Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P50620 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D2D4B914B97BBFA6

FASTA70080,689
        10         20         30         40         50         60 
MSQNQVPKWI QLNNEIMIQK DGKFQFDKDK EAVHSYFVDY INQNTVFFHN LKEKLDYLVE 

        70         80         90        100        110        120 
NQYYEEEFLS LYSFEDIKEV FKTAYAKKFR FPSFMSAFKF YNDYALKTND KKKILERYED 

       130        140        150        160        170        180 
RISIVALFFA NGDTEKAKEY VNLMINQEYQ PSTPTFLNAG RKRRGELVSC FLLEVNDSLN 

       190        200        210        220        230        240 
DISRAIDISM QLSKLGGGVS LNLSKLRAKG EAIKDVENAT KGVVGVMKLL DNAFRYADQM 

       250        260        270        280        290        300 
GQRQGSGAAY LNIFHRDIND FLDTKKISAD EDVRVKTLSI GVVIPDKFVE LAREDKAAYV 

       310        320        330        340        350        360 
FYPHTIYKEY GQHMDEMDMN EMYDKFVDNP RVKKEKINPR KLLEKLAMLR SESGYPYIMF 

       370        380        390        400        410        420 
QDNVNKVHAN NHISKVKFSN LCSEVLQASQ VSSYTDYDEE DEIGLDISCN LGSLNILNVM 

       430        440        450        460        470        480 
EHKSIEKTVK LATDSLTHVS ETTDIRNAPA VRRANKAMKS IGLGAMNLHG YLAQNGIAYE 

       490        500        510        520        530        540 
SPEARDFANT FFMMVNFYSI QRSAEIAKEK GETFDQYEGS TYATGEYFDK YVSTDFSPKY 

       550        560        570        580        590        600 
EKIANLFEGM HIPTTEDWKK LKAFVAEHGM YHSYRLCIAP TGSISYVQSS TASVMPIMER 

       610        620        630        640        650        660 
IEERTYGNSK TYYPMPGLAS NNWFFYKEAY DMDMFKVVDM IATIQQHIDQ GISFTLFLKD 

       670        680        690        700 
TMTTRDLNRI DLYAHHRGIK TIYYARTKDT GQDSCLSCVV 

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis genes for ribonucleotide reductase are similar to the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae."
Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.
Microbiology 142:2995-3004(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z68500 Genomic DNA. Translation: CAA92810.1.
AL009126 Genomic DNA. Translation: CAB13622.1.
PIRB69667.
RefSeqNP_389620.1. NC_000964.3.

3D structure databases

ProteinModelPortalP50620.
SMRP50620. Positions 2-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU17380.

Proteomic databases

PaxDbP50620.
PRIDEP50620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13622; CAB13622; BSU17380.
GeneID940091.
KEGGbsu:BSU17380.
PATRIC18975287. VBIBacSub10457_1835.

Organism-specific databases

GenoListBSU17380. [Micado]

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000246165.
KOK00525.
OMAIYYIRIR.
OrthoDBEOG6J48HC.
PhylomeDBP50620.

Enzyme and pathway databases

BioCycBSUB:BSU17380-MONOMER.
UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR026459. RNR_1b_NrdE.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR013554. RNR_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
PF08343. RNR_N. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
TIGR04170. RNR_1b_NrdE. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_BACSU
AccessionPrimary (citable) accession number: P50620
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 103 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList