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P0CH00

- RIR1B_MYCS2

UniProt

P0CH00 - RIR1B_MYCS2

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Protein

Ribonucleoside-diphosphate reductase subunit alpha 2

Gene

nrdE2

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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 sitei169 – 1691SubstrateBy similarity
Sitei186 – 1861Important for hydrogen atom transferBy similarity
Sitei193 – 1931Allosteric effector bindingBy similarity
Binding sitei214 – 2141Substrate; via amide nitrogenBy similarity
Sitei223 – 2231Allosteric effector bindingBy similarity
Active sitei394 – 3941Proton acceptorBy similarity
Active sitei396 – 3961Cysteine radical intermediateBy similarity
Active sitei398 – 3981Proton acceptorBy similarity
Sitei423 – 4231Important for hydrogen atom transferBy similarity
Sitei700 – 7001Important for electron transferBy similarity
Sitei701 – 7011Important for electron transferBy similarity
Sitei717 – 7171Interacts with thioredoxin/glutaredoxinBy similarity
Sitei720 – 7201Interacts 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 2 (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase R1 subunit 2
Gene namesi
Name:nrdE2
Ordered Locus Names:MSMEG_2299, MSMEI_2241
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Ribonucleoside-diphosphate reductase subunit alpha 2PRO_0000396104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi186 ↔ 423Redox-activeBy similarity
Cross-linki310 – 310Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Disulfide bond, Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1862Substrate bindingBy similarity
Regioni394 – 3985Substrate bindingBy similarity
Regioni596 – 6005Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000246165.
KOiK00525.

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.

P0CH00-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPTVTAAEP VTTTGHVLPG EADYHALNAM LNLYDADGKI QFEKDREAAK
60 70 80 90 100
QYFLQHVNQN TVFFHSQDEK LDYLIENEYY EREVLDQYSR DFIKSLLDRA
110 120 130 140 150
YAKKFRFPTF LGAFKYYTSY TLKTFDGKRY LERFEDRVVM VALTLAAGDT
160 170 180 190 200
ELAEKLVDEI IDGRFQPATP TFLNSGKKQR GEPVSCFLLR IEDNMESIGR
210 220 230 240 250
SINSALQLSK RGGGVALLLS NIREHGAPIK NIENQSSGVI PIMKLLEDSF
260 270 280 290 300
SYANQLGARQ GAGAVYLHAH HPDIYRFLDT KRENADEKIR IKTLSLGVVI
310 320 330 340 350
PDITFELAKK NEDMYLFSPY DVERVYGVPF ADVSVTEKYY EMVDDARIRK
360 370 380 390 400
TKINAREFFQ TLAELQFESG YPYIMFEDTV NRSNPIAGKI THSNLCSEIL
410 420 430 440 450
QVSTPSEFND DLSYAKVGKD ISCNLGSLNI AKAMDSPDFA QTIEVAIRAL
460 470 480 490 500
TAVSDQTHIT SVPSIEQGNN DSHAIGLGQM NLHGYLARER IYYGSEEGID
510 520 530 540 550
FTNIYFYTVL FHALRASNKI AIERGTHFKG FEKSKYASGE FFDKYTDQVW
560 570 580 590 600
EPKTDKVRRL FADADIHIPT QDDWKQLKES VQKHGIYNQN LQAVPPTGSI
610 620 630 640 650
SYINHSTSSI HPVASKIEIR KEGKIGRVYY PAPYMTNDNL DYYQDAYEIG
660 670 680 690 700
YEKIIDTYAA ATQHVDQGLS LTLFFKDTAT TRDVNKAQIY AWRKGIKTLY
710 720
YIRLRQMALE GTEVEGCVSC ML
Length:722
Mass (Da):82,106
Last modified:August 10, 2010 - v1
Checksum:i9D24EFB724737F9A
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK70217.1. Different initiation.
CP001663 Genomic DNA. Translation: AFP38711.1.
RefSeqiWP_014876938.1. NC_018289.1.
YP_006565765.1. NC_018289.1.
YP_006567006.1. NC_018289.1.
YP_885419.1. NC_008596.1.
YP_886648.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK70217; ABK70217; MSMEG_2299.
AFP38711; AFP38711; MSMEI_2241.
GeneIDi4531391.
4535428.
KEGGimsm:MSMEG_1019.
msm:MSMEG_2299.
PATRICi18074490. VBIMycSme59918_1006.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK70217.1 . Different initiation.
CP001663 Genomic DNA. Translation: AFP38711.1 .
RefSeqi WP_014876938.1. NC_018289.1.
YP_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

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK70217 ; ABK70217 ; MSMEG_2299 .
AFP38711 ; AFP38711 ; MSMEI_2241 .
GeneIDi 4531391.
4535428.
KEGGi msm:MSMEG_1019.
msm:MSMEG_2299.
PATRICi 18074490. VBIMycSme59918_1006.

Phylogenomic databases

HOGENOMi HOG000246165.
KOi K00525.

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

« Hide 'large scale' publications
  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. Cited for: PUPYLATION AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRIR1B_MYCS2
AccessioniPrimary (citable) accession number: P0CH00
Secondary accession number(s): A0QR81, I7F7C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: November 26, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

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