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Protein

Vitamin B12-dependent ribonucleotide reductase

Gene

nrdJ

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

adenosylcob(III)alaminBy similarityNote: 5'-deoxyadenosylcobalamine (coenzyme B12).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei142SubstrateBy similarity1
Binding sitei187Substrate; via amide nitrogenBy similarity1
Active sitei363Proton acceptorBy similarity1
Active sitei365Cysteine radical intermediateBy similarity1
Active sitei367Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA synthesis

Keywords - Ligandi

Cobalamin, Cobalt, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin B12-dependent ribonucleotide reductase (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase NrdJ
Gene namesi
Name:nrdJ
Ordered Locus Names:SAV_2461
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
Proteomesi
  • UP000000428 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002316611 – 964Vitamin B12-dependent ribonucleotide reductaseAdd BLAST964

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi159 ↔ 376Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi227882.SAV_2461.

Structurei

3D structure databases

ProteinModelPortaliQ82KE2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 159Substrate bindingBy similarity2
Regioni363 – 367Substrate bindingBy similarity5
Regioni553 – 557Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105BZH. Bacteria.
COG0209. LUCA.
HOGENOMiHOG000021771.
KOiK00525.
OMAiGVEHGYF.
OrthoDBiPOG091H0FGZ.

Family and domain databases

InterProiIPR013678. RNR_2_N.
IPR000788. RNR_lg_C.
IPR013344. RNR_NrdJ/NrdZ.
[Graphical view]
PfamiPF08471. Ribonuc_red_2_N. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
TIGRFAMsiTIGR02504. NrdJ_Z. 1 hit.

Sequencei

Sequence statusi: Complete.

Q82KE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTETASGPAR GSRAKGTKAK GLRIERIHTT PGVHPYDEVE WARRDVVMTN
60 70 80 90 100
WRDGSVNFEQ RGVEFPDFWS VNAVNIVTSK YFRGAVGTPQ REVSLRQLID
110 120 130 140 150
RIVKTYRKAG EDYKYFASPA DAEIFEHELA YALLHQIFSF NSPVWFNVGT
160 170 180 190 200
PQPQQVSACF ILAVDDSMES ILDWYKEEGM IFKGGSGAGL NLSRIRSSKE
210 220 230 240 250
LLSSGGNASG PVSFMRGADA SAGTIKSGGA TRRAAKMVIL DVDHPDIEDF
260 270 280 290 300
IETKVKEEEK IRALRDAGFD MDLGGDDITS VQYQNANNSV RVNDTFMKAV
310 320 330 340 350
EEGGKFGLTS RMTGEVIEEV DAKSLFRKMA EAAWACADPG IQYDDTINHW
360 370 380 390 400
HTCPESGRIN GSNPCSEYMH LDNTSCNLAS LNLMKFLKDD GKGRQSFEVE
410 420 430 440 450
RFAKVVELVI TAMDISICFA DFPTQKIGEN TRAFRQLGIG YANLGALLMA
460 470 480 490 500
TGHAYDSDGG RALAGAITSL MTGTSYKRSA ELAAVVGPYD GYARNAQPHQ
510 520 530 540 550
RVMKQHSDAN GVAVRVDDLD TPIWAAATEA WQDVLHLGEK NGFRNAQASV
560 570 580 590 600
IAPTGTIGLA MSCDTTGLEP DLALVKFKKL VGGGSMQIVN GTVPQALRRL
610 620 630 640 650
GYQEEQIEAI VAHIAENGNV IDAPGLKHEH YEVFDCAMGE RSISAMGHVR
660 670 680 690 700
MMAAIQPWIS GALSKTVNLP ETATVEDVEE VYFEAWKMGV KALAIYRDNC
710 720 730 740 750
KVGQPLSAKK KETEKAEVTA KTEATIREAV EKVVEYRPVR KRLPKGRPGI
760 770 780 790 800
TTSFTVGGAE GYMTANSYPD DGLGEVFLKM SKQGSTLAGM MDAFSIAVSV
810 820 830 840 850
GLQYGVPLET YVSKFTNMRF EPAGMTDDPD VRMAQSIVDY IFRRLALDFL
860 870 880 890 900
PFETRSALGI HSAEERQRHL ETGSYEPSDD VDMDVEGLAQ SAPRAQELKA
910 920 930 940 950
VATPKAEVAA AVPAPKQAHT SAELVEMQLG IQADAPLCFS CGTKMQRAGS
960
CYICEGCGST SGCS
Length:964
Mass (Da):105,012
Last modified:June 1, 2003 - v1
Checksum:i2C634475A49C6B42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC70172.1.
RefSeqiWP_010983898.1. NZ_JZJK01000086.1.

Genome annotation databases

EnsemblBacteriaiBAC70172; BAC70172; SAVERM_2461.
KEGGisma:SAV_2461.
PATRICi23718421. VBIStrAve112782_2628.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC70172.1.
RefSeqiWP_010983898.1. NZ_JZJK01000086.1.

3D structure databases

ProteinModelPortaliQ82KE2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227882.SAV_2461.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC70172; BAC70172; SAVERM_2461.
KEGGisma:SAV_2461.
PATRICi23718421. VBIStrAve112782_2628.

Phylogenomic databases

eggNOGiENOG4105BZH. Bacteria.
COG0209. LUCA.
HOGENOMiHOG000021771.
KOiK00525.
OMAiGVEHGYF.
OrthoDBiPOG091H0FGZ.

Family and domain databases

InterProiIPR013678. RNR_2_N.
IPR000788. RNR_lg_C.
IPR013344. RNR_NrdJ/NrdZ.
[Graphical view]
PfamiPF08471. Ribonuc_red_2_N. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
TIGRFAMsiTIGR02504. NrdJ_Z. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNRDJ_STRAW
AccessioniPrimary (citable) accession number: Q82KE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.