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Q9CBQ0

- RIR1_MYCLE

UniProt

Q9CBQ0 - RIR1_MYCLE

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Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdE

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 sitei168 – 1681SubstrateBy similarity
Sitei185 – 1851Important for hydrogen atom transferBy similarity
Sitei192 – 1921Allosteric effector bindingBy similarity
Binding sitei213 – 2131Substrate; via amide nitrogenBy similarity
Sitei222 – 2221Allosteric effector bindingBy similarity
Active sitei393 – 3931Proton acceptorBy similarity
Active sitei395 – 3951Cysteine radical intermediateBy similarity
Active sitei397 – 3971Proton acceptorBy similarity
Sitei422 – 4221Important for hydrogen atom transferBy similarity
Sitei699 – 6991Important for electron transferBy similarity
Sitei700 – 7001Important for electron transferBy similarity
Sitei716 – 7161Interacts with thioredoxin/glutaredoxinBy similarity
Sitei719 – 7191Interacts 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:ML1734
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000806: Chromosome

Organism-specific databases

LepromaiML1734.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi185 ↔ 422Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Protein-protein interaction databases

STRINGi272631.ML1734.

Structurei

3D structure databases

ProteinModelPortaliQ9CBQ0.
SMRiQ9CBQ0. Positions 16-706.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1852Substrate bindingBy similarity
Regioni393 – 3975Substrate bindingBy similarity
Regioni595 – 5995Substrate 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.

Q9CBQ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPTATAEPV TASTHMLSNE TDYHALNAML NLYDADGKIQ FDKDVLAARQ
60 70 80 90 100
FFLQHVNQNT VFFHNQDEKL DYLIRENYYE REVLDQYSRN FVKSLLDRAY
110 120 130 140 150
AKKFRFSTFL GAFKYYTSYT LKTFDGKRYL ERLEDRVCMV ALTLAAGDTG
160 170 180 190 200
LAEKLVDEII DGRFQPATPT FLNSGKKQRG EPVSCFLLRI EDNMESIGRS
210 220 230 240 250
VNSALQLSKR GGGVALLLSN IREHGAPIKN IEHQSSGVIP IMKLLEDAFS
260 270 280 290 300
YANQLGARQG AGAVYLHAHH PDIYRFLDTK RENADEKIRI KTLSLGVIIP
310 320 330 340 350
DITFELAKRN EDMYLFSSYD VERVYEVPFA DISVTEKYYE MLDDARIRKT
360 370 380 390 400
KIKAREFFQK LAELQFESGY PYVMFEDTVN RANPIEGKIT HSNLCSEILQ
410 420 430 440 450
VSTPSLFNDD LSYAKVGKDI SCNLGSLNIA KTMDSPDFAQ TVEVAIRALT
460 470 480 490 500
AVSDQTHIKS VPSIEQGNND SHAIGLGQMN LHGYLSREGI FYGSEEGVDF
510 520 530 540 550
TNIYFYTVLF HVLLASNSIA IERGTFFKGF ERSKYASGEF FDKYIEQTWE
560 570 580 590 600
PKTDKVRQLF AEAAIRIPTQ NDWKRLKELV VAHGIYNQNL QAVPPTGSIS
610 620 630 640 650
YINHSTSSIH PIVSKVEIRK EGKIGRVYYP APYMTNDNLQ YYQDAYEIGY
660 670 680 690 700
QKIIDTYAAA TQHVDQGLSL TLFFKDTATT RDVNKAQIYA WRKGIKTLYY
710 720
IRLRQMALEG TEVEGCVSCT L
Length:721
Mass (Da):82,024
Last modified:August 29, 2001 - v2
Checksum:i22B365A016228872
GO

Sequence cautioni

The sequence CAC30687.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583923 Genomic DNA. Translation: CAC30687.1. Different initiation.
PIRiH87125.
RefSeqiNP_302195.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC30687; CAC30687; CAC30687.
GeneIDi910759.
KEGGimle:ML1734.
PATRICi18056662. VBIMycLep78757_3260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583923 Genomic DNA. Translation: CAC30687.1 . Different initiation.
PIRi H87125.
RefSeqi NP_302195.1. NC_002677.1.

3D structure databases

ProteinModelPortali Q9CBQ0.
SMRi Q9CBQ0. Positions 16-706.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272631.ML1734.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC30687 ; CAC30687 ; CAC30687 .
GeneIDi 910759.
KEGGi mle:ML1734.
PATRICi 18056662. VBIMycLep78757_3260.

Organism-specific databases

Lepromai ML1734.

Phylogenomic databases

eggNOGi COG0209.
HOGENOMi HOG000246165.
KOi K00525.
OrthoDBi EOG6J48HC.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

InterProi IPR013346. NrdE_NrdA.
IPR026459. RNR_1b_NrdE.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR013554. RNR_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
PF08343. RNR_N. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
TIGR04170. RNR_1b_NrdE. 1 hit.
PROSITEi PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiRIR1_MYCLE
AccessioniPrimary (citable) accession number: Q9CBQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: October 29, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3