O69981 (NRDJ_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	967 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA synthesis
Ligand	Cobalamin Cobalt Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 967	967	Vitamin B12-dependent ribonucleotide reductase		PRO_0000229029
Sites
	Active site	160	1	By similarity
	Active site	366	1	By similarity
	Active site	377	1	By similarity
	Active site	960	1	By similarity
	Active site	966	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O69981 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 1A6522C328673A29	FASTA	967	105,285
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	T35125.
RefSeq	NP_629929.1. NC_003888.3.
3D structure databases
ProteinModelPortal	O69981.
ModBase	Search...
Protein-protein interaction databases
STRING	100226.SCO5805.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAA18341; CAA18341; CAA18341.
GeneID	1101247.
KEGG	sco:SCO5805.
PATRIC	23741500. VBIStrCoe124346_5897.
Phylogenomic databases
eggNOG	COG0209.
HOGENOM	HOG000021771.
KO	K00525.
OMA	FLWRSVP.
ProtClustDB	PRK06556.
Family and domain databases
InterPro	IPR013678. RNR_2_N. IPR000788. RNR_lg_C. IPR013344. RNR_NrdJ/NrdZ. IPR024434. TSCPD_dom. [Graphical view]
Pfam	PF08471. Ribonuc_red_2_N. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF12637. TSCPD. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
TIGRFAMs	TIGR02504. NrdJ_Z. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NRDJ_STRCO

Accession

Primary (citable) accession number: O69981

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program