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P0CH00 (RIR1B_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 2

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase R1 subunit 2
Gene names
Name:nrdE2
Ordered Locus Names:MSMEG_2299, MSMEI_2241
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length722 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.

Miscellaneous

Pupylation of this protein has been demonstrated, although it is unknown if the protein concerned is the product of this gene, of the identical gene MSMEG_1019 (AC P0CG99), or of both genes.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Sequence caution

The sequence ABK70217.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 722722Ribonucleoside-diphosphate reductase subunit alpha 2
PRO_0000396104

Regions

Region185 – 1862Substrate binding By similarity
Region394 – 3985Substrate binding By similarity
Region596 – 6005Substrate binding By similarity

Sites

Active site3941Proton acceptor By similarity
Active site3961Cysteine radical intermediate By similarity
Active site3981Proton acceptor By similarity
Binding site1691Substrate By similarity
Binding site2141Substrate; via amide nitrogen By similarity
Site1861Important for hydrogen atom transfer By similarity
Site1931Allosteric effector binding By similarity
Site2231Allosteric effector binding By similarity
Site4231Important for hydrogen atom transfer By similarity
Site7001Important for electron transfer By similarity
Site7011Important for electron transfer By similarity
Site7171Interacts with thioredoxin/glutaredoxin By similarity
Site7201Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond186 ↔ 423Redox-active By similarity
Cross-link310Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Sequences

Sequence LengthMass (Da)Tools
P0CH00 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 9D24EFB724737F9A

FASTA72282,106
        10         20         30         40         50         60 
MPPTVTAAEP VTTTGHVLPG EADYHALNAM LNLYDADGKI QFEKDREAAK QYFLQHVNQN 

        70         80         90        100        110        120 
TVFFHSQDEK LDYLIENEYY EREVLDQYSR DFIKSLLDRA YAKKFRFPTF LGAFKYYTSY 

       130        140        150        160        170        180 
TLKTFDGKRY LERFEDRVVM VALTLAAGDT ELAEKLVDEI IDGRFQPATP TFLNSGKKQR 

       190        200        210        220        230        240 
GEPVSCFLLR IEDNMESIGR SINSALQLSK RGGGVALLLS NIREHGAPIK NIENQSSGVI 

       250        260        270        280        290        300 
PIMKLLEDSF SYANQLGARQ GAGAVYLHAH HPDIYRFLDT KRENADEKIR IKTLSLGVVI 

       310        320        330        340        350        360 
PDITFELAKK NEDMYLFSPY DVERVYGVPF ADVSVTEKYY EMVDDARIRK TKINAREFFQ 

       370        380        390        400        410        420 
TLAELQFESG YPYIMFEDTV NRSNPIAGKI THSNLCSEIL QVSTPSEFND DLSYAKVGKD 

       430        440        450        460        470        480 
ISCNLGSLNI AKAMDSPDFA QTIEVAIRAL TAVSDQTHIT SVPSIEQGNN DSHAIGLGQM 

       490        500        510        520        530        540 
NLHGYLARER IYYGSEEGID FTNIYFYTVL FHALRASNKI AIERGTHFKG FEKSKYASGE 

       550        560        570        580        590        600 
FFDKYTDQVW EPKTDKVRRL FADADIHIPT QDDWKQLKES VQKHGIYNQN LQAVPPTGSI 

       610        620        630        640        650        660 
SYINHSTSSI HPVASKIEIR KEGKIGRVYY PAPYMTNDNL DYYQDAYEIG YEKIIDTYAA 

       670        680        690        700        710        720 
ATQHVDQGLS LTLFFKDTAT TRDVNKAQIY AWRKGIKTLY YIRLRQMALE GTEVEGCVSC 


ML 

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Expansion of the mycobacterial 'PUPylome'."
Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V., Barry C.E. III, Bark S., Dorrestein P.C.
Mol. Biosyst. 6:376-385(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PUPYLATION AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK70217.1. Different initiation.
CP001663 Genomic DNA. Translation: AFP38711.1.
RefSeqYP_006565765.1. NC_018289.1.
YP_006567006.1. NC_018289.1.
YP_885419.1. NC_008596.1.
YP_886648.1. NC_008596.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK70217; ABK70217; MSMEG_2299.
AFP38711; AFP38711; MSMEI_2241.
GeneID4531391.
4535428.
KEGGmsg:MSMEI_0990.
msg:MSMEI_2241.
msm:MSMEG_1019.
msm:MSMEG_2299.
PATRIC18074490. VBIMycSme59918_1006.

Phylogenomic databases

HOGENOMHOG000246165.
KOK00525.

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. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
TIGR04170. RNR_1b_NrdE. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1B_MYCS2
AccessionPrimary (citable) accession number: P0CH00
Secondary accession number(s): A0QR81, I7F7C8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: July 9, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways