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P0A5W9 (RIR1_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Mb3077c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Induction

Induced in response to the thiol oxidant diamide. Ref.2

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Sequence caution

The sequence CAD96764.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 725725Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187219

Regions

Region188 – 1892Substrate binding By similarity
Region397 – 4015Substrate binding By similarity
Region599 – 6035Substrate binding By similarity

Sites

Active site3971Proton acceptor By similarity
Active site3991Cysteine radical intermediate By similarity
Active site4011Proton acceptor By similarity
Binding site1721Substrate By similarity
Binding site2171Substrate; via amide nitrogen By similarity
Site1891Important for hydrogen atom transfer By similarity
Site1961Allosteric effector binding By similarity
Site2261Allosteric effector binding By similarity
Site4261Important for hydrogen atom transfer By similarity
Site7031Important for electron transfer By similarity
Site7041Important for electron transfer By similarity
Site7201Interacts with thioredoxin/glutaredoxin By similarity
Site7231Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond189 ↔ 426Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A5W9 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 38C315D149331D55

FASTA72582,441
        10         20         30         40         50         60 
MPPTVIAEPV ASGAHASYSG GPGETDYHAL NAMLNLYDAD GKIQFDKDRE AAHQYFLQHV 

        70         80         90        100        110        120 
NQNTVFFHNQ DEKLDYLIRE NYYEREVLDQ YSRNFVKTLL DRAYAKKFRF PTFLGAFKYY 

       130        140        150        160        170        180 
TSYTLKTFDG KRYLERFEDR VVMVALTLAA GDTALAELLV DEIIDGRFQP ATPTFLNSGK 

       190        200        210        220        230        240 
KQRGEPVSCF LLRVEDNMES IGRSINSALQ LSKRGGGVAL LLTNIREHGA PIKNIENQSS 

       250        260        270        280        290        300 
GVIPIMKLLE DAFSYANQLG ARQGAGAVYL HAHHPDIYRF LDTKRENADE KIRIKTLSLG 

       310        320        330        340        350        360 
VVIPDITFEL AKRNDDMYLF SPYDVERVYG VPFADISVTE KYYEMVDDAR IRKTKIKARE 

       370        380        390        400        410        420 
FFQTLAELQF ESGYPYIMFE DTVNRANPID GKITHSNLCS EILQVSTPSL FNEDLSYAKV 

       430        440        450        460        470        480 
GKDISCNLGS LNIAKTMDSP DFAQTIEVAI RALTAVSDQT HIKSVPSIEQ GNNDSHAIGL 

       490        500        510        520        530        540 
GQMNLHGYLA RERIFYGSDE GIDFTNIYFY TVLYHALRAS NRIAIERGTH FKGFERSKYA 

       550        560        570        580        590        600 
SGEFFDKYTD QIWEPKTQKV RQLFADAGIR IPTQDDWRRL KESVQAHGIY NQNLQAVPPT 

       610        620        630        640        650        660 
GSISYINHST SSIHPIVSKV EIRKEGKIGR VYYPAPYMTN DNLEYYEDAY EIGYEKIIDT 

       670        680        690        700        710        720 
YAAATQHVDQ GLSLTLFFKD TATTRDVNKA QIYAWRKGIK TLYYIRLRQM ALEGTEVEGC 


VSCML

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract]
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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
Strain: BCG / Pasteur.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248344 Genomic DNA. Translation: CAD96764.1. Different initiation.
RefSeqNP_856722.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A5W9.
SMRP0A5W9. Positions 26-710.
ModBaseSearch...

Protein-protein interaction databases

STRING233413.Mb3077c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96764; CAD96764; Mb3077c.
GeneID1093421.
KEGGmbo:Mb3077c.
PATRIC18008502. VBIMycBov88188_3381.

Organism-specific databases

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_MYCBO
AccessionPrimary (citable) accession number: P0A5W9
Secondary accession number(s): O53296, P50640
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 57 of the entry and version 1 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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