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P0CG99

- RIR1A_MYCS2

UniProt

P0CG99 - RIR1A_MYCS2

Protein

Ribonucleoside-diphosphate reductase subunit alpha 1

Gene

nrdE1

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (10 Aug 2010)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-1019-MONOMER.
    MSME246196:GJ4Y-2299-MONOMER.
    RETL1328306-WGS:GSTH-3791-MONOMER.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit alpha 1 (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase R1 subunit 1
    Gene namesi
    Name:nrdE1
    Ordered Locus Names:MSMEG_1019, MSMEI_0990
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 722722Ribonucleoside-diphosphate reductase subunit alpha 1PRO_0000396103Add
    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.
    OrthoDBiEOG6J48HC.

    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.

    P0CG99-1 [UniParc]FASTAAdd to Basket

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    MPPTVTAAEP VTTTGHVLPG EADYHALNAM LNLYDADGKI QFEKDREAAK    50
    QYFLQHVNQN TVFFHSQDEK LDYLIENEYY EREVLDQYSR DFIKSLLDRA 100
    YAKKFRFPTF LGAFKYYTSY TLKTFDGKRY LERFEDRVVM VALTLAAGDT 150
    ELAEKLVDEI IDGRFQPATP TFLNSGKKQR GEPVSCFLLR IEDNMESIGR 200
    SINSALQLSK RGGGVALLLS NIREHGAPIK NIENQSSGVI PIMKLLEDSF 250
    SYANQLGARQ GAGAVYLHAH HPDIYRFLDT KRENADEKIR IKTLSLGVVI 300
    PDITFELAKK NEDMYLFSPY DVERVYGVPF ADVSVTEKYY EMVDDARIRK 350
    TKINAREFFQ TLAELQFESG YPYIMFEDTV NRSNPIAGKI THSNLCSEIL 400
    QVSTPSEFND DLSYAKVGKD ISCNLGSLNI AKAMDSPDFA QTIEVAIRAL 450
    TAVSDQTHIT SVPSIEQGNN DSHAIGLGQM NLHGYLARER IYYGSEEGID 500
    FTNIYFYTVL FHALRASNKI AIERGTHFKG FEKSKYASGE FFDKYTDQVW 550
    EPKTDKVRRL FADADIHIPT QDDWKQLKES VQKHGIYNQN LQAVPPTGSI 600
    SYINHSTSSI HPVASKIEIR KEGKIGRVYY PAPYMTNDNL DYYQDAYEIG 650
    YEKIIDTYAA ATQHVDQGLS LTLFFKDTAT TRDVNKAQIY AWRKGIKTLY 700
    YIRLRQMALE GTEVEGCVSC ML 722
    Length:722
    Mass (Da):82,106
    Last modified:August 10, 2010 - v1
    Checksum:i9D24EFB724737F9A
    GO

    Sequence cautioni

    The sequence ABK71849.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71849.1. Different initiation.
    CP001663 Genomic DNA. Translation: AFP37470.1.
    RefSeqiYP_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

    EnsemblBacteriaiABK71849; ABK71849; MSMEG_1019.
    AFP37470; AFP37470; MSMEI_0990.
    GeneIDi4531391.
    4535428.
    KEGGimsg:MSMEI_0990.
    msg:MSMEI_2241.
    msm:MSMEG_1019.
    msm:MSMEG_2299.
    PATRICi18074490. VBIMycSme59918_1006.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71849.1 . Different initiation.
    CP001663 Genomic DNA. Translation: AFP37470.1 .
    RefSeqi 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 ABK71849 ; ABK71849 ; MSMEG_1019 .
    AFP37470 ; AFP37470 ; MSMEI_0990 .
    GeneIDi 4531391.
    4535428.
    KEGGi msg:MSMEI_0990.
    msg:MSMEI_2241.
    msm:MSMEG_1019.
    msm:MSMEG_2299.
    PATRICi 18074490. VBIMycSme59918_1006.

    Phylogenomic databases

    HOGENOMi HOG000246165.
    KOi K00525.
    OrthoDBi EOG6J48HC.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci MSME246196:GJ4Y-1019-MONOMER.
    MSME246196:GJ4Y-2299-MONOMER.
    RETL1328306-WGS:GSTH-3791-MONOMER.

    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

    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 nameiRIR1A_MYCS2
    AccessioniPrimary (citable) accession number: P0CG99
    Secondary accession number(s): A0QR81, I7F7C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 10, 2010
    Last sequence update: August 10, 2010
    Last modified: October 1, 2014
    This is version 30 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_2299 (AC P0CH00), 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