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Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdE

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721SubstrateBy similarity
Sitei189 – 1891Important for hydrogen atom transferBy similarity
Sitei196 – 1961Allosteric effector bindingBy similarity
Binding sitei217 – 2171Substrate; via amide nitrogenBy similarity
Sitei226 – 2261Allosteric effector bindingBy similarity
Active sitei397 – 3971Proton acceptorBy similarity
Active sitei399 – 3991Cysteine radical intermediateBy similarity
Active sitei401 – 4011Proton acceptorBy similarity
Sitei426 – 4261Important for hydrogen atom transferBy similarity
Sitei703 – 7031Important for electron transferBy similarity
Sitei704 – 7041Important for electron transferBy similarity
Sitei720 – 7201Interacts with thioredoxin/glutaredoxinBy similarity
Sitei723 – 7231Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase subunit alpha (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase R1 subunit
Gene namesi
Name:nrdE
Ordered Locus Names:Mb3077c
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi189 ↔ 426Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Induced in response to the thiol oxidant diamide.1 Publication

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Protein-protein interaction databases

STRINGi233413.Mb3077c.

Structurei

3D structure databases

ProteinModelPortaliP0A5W9.
SMRiP0A5W9. Positions 26-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 1892Substrate bindingBy similarity
Regioni397 – 4015Substrate bindingBy similarity
Regioni599 – 6035Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000246165.
KOiK00525.
OrthoDBiEOG6J48HC.

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR026459. RNR_1b_NrdE.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR013554. RNR_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
PF08343. RNR_N. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
TIGR04170. RNR_1b_NrdE. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A5W9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPTVIAEPV ASGAHASYSG GPGETDYHAL NAMLNLYDAD GKIQFDKDRE
60 70 80 90 100
AAHQYFLQHV NQNTVFFHNQ DEKLDYLIRE NYYEREVLDQ YSRNFVKTLL
110 120 130 140 150
DRAYAKKFRF PTFLGAFKYY TSYTLKTFDG KRYLERFEDR VVMVALTLAA
160 170 180 190 200
GDTALAELLV DEIIDGRFQP ATPTFLNSGK KQRGEPVSCF LLRVEDNMES
210 220 230 240 250
IGRSINSALQ LSKRGGGVAL LLTNIREHGA PIKNIENQSS GVIPIMKLLE
260 270 280 290 300
DAFSYANQLG ARQGAGAVYL HAHHPDIYRF LDTKRENADE KIRIKTLSLG
310 320 330 340 350
VVIPDITFEL AKRNDDMYLF SPYDVERVYG VPFADISVTE KYYEMVDDAR
360 370 380 390 400
IRKTKIKARE FFQTLAELQF ESGYPYIMFE DTVNRANPID GKITHSNLCS
410 420 430 440 450
EILQVSTPSL FNEDLSYAKV GKDISCNLGS LNIAKTMDSP DFAQTIEVAI
460 470 480 490 500
RALTAVSDQT HIKSVPSIEQ GNNDSHAIGL GQMNLHGYLA RERIFYGSDE
510 520 530 540 550
GIDFTNIYFY TVLYHALRAS NRIAIERGTH FKGFERSKYA SGEFFDKYTD
560 570 580 590 600
QIWEPKTQKV RQLFADAGIR IPTQDDWRRL KESVQAHGIY NQNLQAVPPT
610 620 630 640 650
GSISYINHST SSIHPIVSKV EIRKEGKIGR VYYPAPYMTN DNLEYYEDAY
660 670 680 690 700
EIGYEKIIDT YAAATQHVDQ GLSLTLFFKD TATTRDVNKA QIYAWRKGIK
710 720
TLYYIRLRQM ALEGTEVEGC VSCML
Length:725
Mass (Da):82,441
Last modified:March 15, 2005 - v1
Checksum:i38C315D149331D55
GO

Sequence cautioni

The sequence CDO44346.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44346.1. Different initiation.
RefSeqiNP_856722.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO44346; CDO44346; Mb3077c.
GeneIDi1093421.
KEGGimbo:Mb3077c.
PATRICi18008502. VBIMycBov88188_3381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44346.1. Different initiation.
RefSeqiNP_856722.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP0A5W9.
SMRiP0A5W9. Positions 26-710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi233413.Mb3077c.

Chemistry

BindingDBiP0A5W9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO44346; CDO44346; Mb3077c.
GeneIDi1093421.
KEGGimbo:Mb3077c.
PATRICi18008502. VBIMycBov88188_3381.

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000246165.
KOiK00525.
OrthoDBiEOG6J48HC.

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR026459. RNR_1b_NrdE.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR013554. RNR_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
PF08343. RNR_N. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
TIGR04170. RNR_1b_NrdE. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.
  2. "Thiol specific oxidative stress response in Mycobacteria."
    Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.
    FEMS Microbiol. Lett. 249:87-94(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
    Strain: BCG / Pasteur.

Entry informationi

Entry nameiRIR1_MYCBO
AccessioniPrimary (citable) accession number: P0A5W9
Secondary accession number(s): O53296, P50640, X2BN79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: April 1, 2015
This is version 67 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

Allosteric enzyme, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.