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P50621 (RIR2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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 beta
EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase small subunit
Gene names
Name:nrdF
Ordered Locus Names:BSU17390
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Cofactor

Binds 2 iron ions per subunit 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 small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Ribonucleoside-diphosphate reductase subunit beta
PRO_0000190469

Sites

Active site1051 By similarity
Metal binding661Iron 1 By similarity
Metal binding971Iron 1 By similarity
Metal binding971Iron 2 By similarity
Metal binding1011Iron 1 By similarity
Metal binding1641Iron 2 By similarity
Metal binding1981Iron 2 By similarity
Metal binding2011Iron 2 By similarity

Secondary structure

1 ..................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50621 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5080C014D2868EEB

FASTA32938,379
        10         20         30         40         50         60 
MTKIYDAANW SKHEDDFTQM FYNQNVKQFW LPEEIALNGD LLTWKYLGKN EQDTYMKVLA 

        70         80         90        100        110        120 
GLTLLDTEQG NTGMPIVAEH VDGHQRKAVL NFMAMMENAV HAKSYSNIFM TLAPTETINE 

       130        140        150        160        170        180 
VFEWVKQNKY LQKKAQMIVG LYKAIQKDDE ISLFKAMVAS VYLESFLFYS GFYYPLYFYG 

       190        200        210        220        230        240 
QGKLMQSGEI INLILRDEAI HGVYVGLLAQ EIYNKQTEEK KAELREFAID LLNQLYENEL 

       250        260        270        280        290        300 
EYTEDLYDQV GLSHDVKKFI RYNANKALMN LGFDPYFEEE DINPIVLNGL NTKTKSHDFF 

       310        320 
SMKGNGYKKA TVEPLKDDDF YFEDEKEQI

« 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z68500 Genomic DNA. Translation: CAA92811.1.
AL009126 Genomic DNA. Translation: CAB13623.1.
PIRC69667.
RefSeqNP_389621.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DR0X-ray1.90A/B1-329[»]
ProteinModelPortalP50621.
SMRP50621. Positions 4-286.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU17390.

Proteomic databases

PaxDbP50621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13623; CAB13623; BSU17390.
GeneID940076.
KEGGbsu:BSU17390.
PATRIC18975289. VBIBacSub10457_1836.

Organism-specific databases

GenoListBSU17390. [Micado]

Phylogenomic databases

eggNOGCOG0208.
HOGENOMHOG000246154.
KOK00526.
OMAIGYKYQR.
ProtClustDBPRK09614.

Enzyme and pathway databases

BioCycBSUB:BSU17390-MONOMER.
UniPathwayUPA00326.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR026494. RNR_1b_NrdF.
IPR026023. RNR_bsu_prok.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
PIRSFPIRSF000355. NrdB. 1 hit.
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
TIGRFAMsTIGR04171. RNR_1b_NrdF. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR2_BACSU
AccessionPrimary (citable) accession number: P50621
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents