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O69981 (NRDJ_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Vitamin B12-dependent ribonucleotide reductase

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase NrdJ
Gene names
Name:nrdJ
Ordered Locus Names:SCO5805
ORF Names:SC4H2.26
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Cofactor

5'-deoxyadenosylcobalamine (coenzyme B12) Probable.

Developmental stage

Expressed during the exponential phase of growth.

Induction

Induced by NrdR. Ref.3

Miscellaneous

Can grow normally using either of its two RNR systems.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase class-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 967967Vitamin B12-dependent ribonucleotide reductase
PRO_0000229029

Regions

Region159 – 1602Substrate binding By similarity
Region364 – 3685Substrate binding By similarity
Region554 – 5585Substrate binding By similarity

Sites

Active site3641Proton acceptor By similarity
Active site3661Cysteine radical intermediate By similarity
Active site3681Proton acceptor By similarity
Binding site1431Substrate By similarity
Binding site1881Substrate; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond160 ↔ 377Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O69981 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 1A6522C328673A29

FASTA967105,285
        10         20         30         40         50         60 
MTETASGPAR SSRAKGTKAG KGLRVERVHT TPGVHPYDEV AWERRDVVMT NWRDGSVNFE 

        70         80         90        100        110        120 
QRGVEFPEFW SVNAVNIVTS KYFRGAVGTP QREVSLKQLI DRIVKTYRKA GEDNKYFASP 

       130        140        150        160        170        180 
ADAEIFEHEL AYALLHQIFS FNSPVWFNVG TPQPQQVSAC FILSVDDSME SILDWYKEEG 

       190        200        210        220        230        240 
MIFKGGSGAG LNLSRIRSSK ELLSSGGNAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVI 

       250        260        270        280        290        300 
LDVDHPDIED FIQTKVKEEE KIRALRDAGF DMDLGGDDIT SVQYQNANNS VRVNDTFMKA 

       310        320        330        340        350        360 
VQDGGKFGLT SRMTGEVIEE VDAKALFRKM AEAAWACADP GIQYDDTINA WHTCPESGRI 

       370        380        390        400        410        420 
NGSNPCSEYM HLDNTSCNLA SLNLMKFLKD DGKGNQSFDA ERFSKVVELV ITAMDISICF 

       430        440        450        460        470        480 
ADFPTQKIGE NTRAFRQLGI GYANLGALLM ATGHAYDSDG GRALAGAITS LMTGTSYRRS 

       490        500        510        520        530        540 
AELAAIVGPY DGYARNAKPH LRVMKQHSDE NAKAVRMDDL DTPIWAAATE AWQDVLRLGE 

       550        560        570        580        590        600 
KNGFRNSQAS VIAPTGTIGL AMSCDTTGLE PDLALVKFKK LVGGGSMQIV NGTVPQALRR 

       610        620        630        640        650        660 
LGYQEEQIEA IVAHIAENGN VIDAPGLKPE HYEVFDCAMG ERSISAMGHV RMMAAIQPWI 

       670        680        690        700        710        720 
SGALSKTVNL PESATVEDVE EVYFEAWKMG VKALAIYRDN CKVGQPLSAK TKTVKDTEKA 

       730        740        750        760        770        780 
EITEKTEAAI RETVEKVVEY RPVRKRLPKG RPGITTSFTV GGAEGYMTAN SYPDDGLGEV 

       790        800        810        820        830        840 
FLKMSKQGST LAGMMDAFSI AVSVGLQYGV PLETYVSKFT NMRFEPAGMT DDPDVRMAQS 

       850        860        870        880        890        900 
IVDYIFRRLA LDFLPFETRS ALGIHSAEER QRHLETGSYE PSDDELDVEG LAQSAPRAQE 

       910        920        930        940        950        960 
LVAVATPKAE AEAAKPAPQQ AHTSAELVEM QLGIQADAPL CFSCGTKMQR AGSCYICEGC 


GSTSGCS 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Streptomyces spp. contain class Ia and class II ribonucleotide reductases: expression analysis of the genes in vegetative growth."
Borovok I., Kreisberg-Zakarin R., Yanko M., Schreiber R., Myslovati M., Aaslund F., Holmgren A., Cohen G., Aharonowitz Y.
Microbiology 148:391-404(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[3]"Alternative oxygen-dependent and oxygen-independent ribonucleotide reductases in Streptomyces: cross-regulation and physiological role in response to oxygen limitation."
Borovok I., Gorovitz B., Yanku M., Schreiber R., Gust B., Chater K., Aharonowitz Y., Cohen G.
Mol. Microbiol. 54:1022-1035(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], REGULATION.
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939125 Genomic DNA. Translation: CAA18341.1.
AM039891 Genomic RNA. Translation: CAJ01782.1.
PIRT35125.
RefSeqNP_629929.1. NC_003888.3.

3D structure databases

ProteinModelPortalO69981.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5805.

Proteomic databases

PRIDEO69981.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA18341; CAA18341; CAA18341.
GeneID1101247.
KEGGsco:SCO5805.
PATRIC23741500. VBIStrCoe124346_5897.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000021771.
KOK00525.
OMATAFDIKF.
OrthoDBEOG6H4K5F.
PhylomeDBO69981.
ProtClustDBPRK06556.

Family and domain databases

InterProIPR013678. RNR_2_N.
IPR000788. RNR_lg_C.
IPR013344. RNR_NrdJ/NrdZ.
IPR024434. TSCPD_dom.
[Graphical view]
PfamPF08471. Ribonuc_red_2_N. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF12637. TSCPD. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
TIGRFAMsTIGR02504. NrdJ_Z. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNRDJ_STRCO
AccessionPrimary (citable) accession number: O69981
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: August 1, 1998
Last modified: April 16, 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