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Q9CBQ0 (RIR1_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase subunit alpha
EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase R1 subunit
Gene names
Name:nrdE
Ordered Locus Names:ML1734
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

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.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187220

Regions

Region184 – 1852Substrate binding By similarity
Region393 – 3975Substrate binding By similarity
Region595 – 5995Substrate binding By similarity

Sites

Active site3931Proton acceptor By similarity
Active site3951Cysteine radical intermediate By similarity
Active site3971Proton acceptor By similarity
Binding site1681Substrate By similarity
Binding site2131Substrate; via amide nitrogen By similarity
Site1851Important for hydrogen atom transfer By similarity
Site1921Allosteric effector binding By similarity
Site2221Allosteric effector binding By similarity
Site4221Important for hydrogen atom transfer By similarity
Site6991Important for electron transfer By similarity
Site7001Important for electron transfer By similarity
Site7161Interacts with thioredoxin/glutaredoxin By similarity
Site7191Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond185 ↔ 422Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CBQ0 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 22B365A016228872

FASTA72182,024
        10         20         30         40         50         60 
MPPTATAEPV TASTHMLSNE TDYHALNAML NLYDADGKIQ FDKDVLAARQ FFLQHVNQNT 

        70         80         90        100        110        120 
VFFHNQDEKL DYLIRENYYE REVLDQYSRN FVKSLLDRAY AKKFRFSTFL GAFKYYTSYT 

       130        140        150        160        170        180 
LKTFDGKRYL ERLEDRVCMV ALTLAAGDTG LAEKLVDEII DGRFQPATPT FLNSGKKQRG 

       190        200        210        220        230        240 
EPVSCFLLRI EDNMESIGRS VNSALQLSKR GGGVALLLSN IREHGAPIKN IEHQSSGVIP 

       250        260        270        280        290        300 
IMKLLEDAFS YANQLGARQG AGAVYLHAHH PDIYRFLDTK RENADEKIRI KTLSLGVIIP 

       310        320        330        340        350        360 
DITFELAKRN EDMYLFSSYD VERVYEVPFA DISVTEKYYE MLDDARIRKT KIKAREFFQK 

       370        380        390        400        410        420 
LAELQFESGY PYVMFEDTVN RANPIEGKIT HSNLCSEILQ VSTPSLFNDD LSYAKVGKDI 

       430        440        450        460        470        480 
SCNLGSLNIA KTMDSPDFAQ TVEVAIRALT AVSDQTHIKS VPSIEQGNND SHAIGLGQMN 

       490        500        510        520        530        540 
LHGYLSREGI FYGSEEGVDF TNIYFYTVLF HVLLASNSIA IERGTFFKGF ERSKYASGEF 

       550        560        570        580        590        600 
FDKYIEQTWE PKTDKVRQLF AEAAIRIPTQ NDWKRLKELV VAHGIYNQNL QAVPPTGSIS 

       610        620        630        640        650        660 
YINHSTSSIH PIVSKVEIRK EGKIGRVYYP APYMTNDNLQ YYQDAYEIGY QKIIDTYAAA 

       670        680        690        700        710        720 
TQHVDQGLSL TLFFKDTATT RDVNKAQIYA WRKGIKTLYY IRLRQMALEG TEVEGCVSCT 


L

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL583923 Genomic DNA. Translation: CAC30687.1. Different initiation.
PIRH87125.
RefSeqNP_302195.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ9CBQ0.
SMRQ9CBQ0. Positions 16-706.
ModBaseSearch...

Protein-protein interaction databases

STRING272631.ML1734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC30687; CAC30687; CAC30687.
GeneID910759.
KEGGmle:ML1734.
PATRIC18056662. VBIMycLep78757_3260.

Organism-specific databases

LepromaML1734.
CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000246165.
KOK00525.
ProtClustDBPRK08188.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR026459. RNR_1b_NrdE.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR013554. RNR_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
PF08343. RNR_N. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. Ribonucleo_red_N. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
TIGR04170. RNR_1b_NrdE. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_MYCLE
AccessionPrimary (citable) accession number: Q9CBQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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