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Reviewed, UniProtKB/Swiss-Prot Q9CBQ0 (RIR1_MYCLE)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier1769 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187220

Sites

Active site1851Hydrogen atom transfer By similarity
Active site3931Proton acceptor By similarity
Active site3951Proton acceptor By similarity
Active site3971Proton acceptor By similarity
Active site4221Hydrogen atom transfer By similarity
Active site6991Electron transfer By similarity
Active site7001Electron transfer By similarity
Site1921Allosteric effector binding By similarity
Site2221Allosteric effector binding 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
Q9CBQ0-1 [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

AL583923 Genomic DNA. Translation: CAC30687.1. Different initiation.
PIRH87125.
RefSeqNP_302195.1.

3D structure databases

SMRQ9CBQ0. Positions 16-706.
ModBaseSearch...

Genome annotation databases

GeneID910759.
GenomeReviewsGene locus ML1734 in contig AL450380_GR.
KEGGmle:ML1734.
NMPDRfig|272631.1.peg.1067.

Organism-specific databases

LepromaML1734.
CMRSearch...

Phylogenomic databases

HOGENOMQ9CBQ0.

Enzyme and pathway databases

BioCycMLEP272631:ML1734-MON.
BRENDA1.17.4.1. 808.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR013509. Ribncl_Rdtase_lsu_N.
IPR000788. Ribncl_red_lg_C.
IPR013554. Ribonucl_Rdtase_N.
[Graphical view]
PANTHERPTHR11573. Ribncl_red_lg_C. 1 hit.
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
PF08343. RNR_N. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
TIGRFAMsTIGR02506. NrdE_NrdA. 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: June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents