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P78027

- RIR1_MYCPN

UniProt

P78027 - RIR1_MYCPN

Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdE

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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 sitei159 – 1591SubstrateBy similarity
    Sitei176 – 1761Important for hydrogen atom transferBy similarity
    Sitei183 – 1831Allosteric effector bindingBy similarity
    Binding sitei204 – 2041Substrate; via amide nitrogenBy similarity
    Sitei213 – 2131Allosteric effector bindingBy similarity
    Active sitei384 – 3841Proton acceptorBy similarity
    Active sitei386 – 3861Cysteine radical intermediateBy similarity
    Active sitei388 – 3881Proton acceptorBy similarity
    Sitei413 – 4131Important for hydrogen atom transferBy similarity
    Sitei694 – 6941Important for electron transferBy similarity
    Sitei695 – 6951Important for electron transferBy similarity
    Sitei716 – 7161Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei719 – 7191Interacts 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

    BioCyciMPNE272634:GJ6Z-341-MONOMER.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit alpha (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase
    Gene namesi
    Name:nrdE
    Ordered Locus Names:MPN_324
    ORF Names:MP512
    OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
    Taxonomic identifieri272634 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
    ProteomesiUP000000808: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 721721Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187218Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi176 ↔ 413Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP78027.

    PTM databases

    PhosSiteiP1011996.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    IntActiP78027. 7 interactions.
    STRINGi272634.MPN324.

    Structurei

    3D structure databases

    ProteinModelPortaliP78027.
    SMRiP78027. Positions 18-700.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1762Substrate bindingBy similarity
    Regioni384 – 3885Substrate bindingBy similarity
    Regioni589 – 5935Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0209.
    KOiK00525.
    OMAiIYYIRIR.
    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.

    P78027-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVKEKIPAF NTQEDLESYI SLNAYTKVYG DFKMDLHAVE AYIQEHVKPK    50
    TKVFHSTKER LDFLVKNDYY DENIINMYSF EQFEEITRKA YAYRFRYANF 100
    MGAFKFYNAY ALKTFDGKWY LENYEDRVVM NVLFLANGNY NKALKLLKQI 150
    ITNRFQPATP TFLNAGRKKR GEFVSCYLLR IEDNMESIGR AITTTLQLSK 200
    RDGGVALLLT NIRESGAPIK KIENQSSGII PIMKLLEDSF SYANQLGQRQ 250
    GAGAVYLHAH HPDVMQFLDT KRENADEKIR IKSLSLGLVI PDITFTLAKN 300
    NEEMALFSPY DVYEEYGKPL SDISVTEMYY ELLANQRIKK TFINARKFFQ 350
    TVAELHFESG YPYILFDDTV NRRNAHPNRI VMSNLCSEIV QPSTPSEFHH 400
    DLAFKKVGND ISCNLGSLNI AKAMESGPEF SELVKLAIES LDLVSRVSNL 450
    ETAPSIQKGN SENHALGLGA MNLHGFLATN QIYYNSPEAI DFTNIFFYTV 500
    AYHAFKASSE LALEKGKFKN FENTKFADGS YFDKYIKVEP DFWTPKTERV 550
    KALFQKYQVE IPTRENWKEL ALNIQKNGLA NSHLLAIAPT GSISYLSSCT 600
    PSLQPVVSPV EVRKEGRLGR IYVPAYQLNK DSYPFYKDGA YELGPEPIIN 650
    IAAAAQQHVD QAISLTLFMT DKATTRDLNK AYIYAFKKGC SSIYYVRVRQ 700
    EVLEDSEDHT IQMQQCEACV I 721
    Length:721
    Mass (Da):82,375
    Last modified:February 1, 1997 - v1
    Checksum:i93CAEA95A2A9E647
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00089 Genomic DNA. Translation: AAB96160.1.
    PIRiS73838.
    RefSeqiNP_110012.1. NC_000912.1.

    Genome annotation databases

    EnsemblBacteriaiAAB96160; AAB96160; MPN_324.
    GeneIDi876946.
    KEGGimpn:MPN324.
    PATRICi20022002. VBIMycPne110_0348.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00089 Genomic DNA. Translation: AAB96160.1 .
    PIRi S73838.
    RefSeqi NP_110012.1. NC_000912.1.

    3D structure databases

    ProteinModelPortali P78027.
    SMRi P78027. Positions 18-700.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P78027. 7 interactions.
    STRINGi 272634.MPN324.

    PTM databases

    PhosSitei P1011996.

    Proteomic databases

    PaxDbi P78027.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB96160 ; AAB96160 ; MPN_324 .
    GeneIDi 876946.
    KEGGi mpn:MPN324.
    PATRICi 20022002. VBIMycPne110_0348.

    Phylogenomic databases

    eggNOGi COG0209.
    KOi K00525.
    OMAi IYYIRIR.
    OrthoDBi EOG6J48HC.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci MPNE272634:GJ6Z-341-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. "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
      Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
      Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29342 / M129.

    Entry informationi

    Entry nameiRIR1_MYCPN
    AccessioniPrimary (citable) accession number: P78027
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Mycoplasma pneumoniae
      Mycoplasma pneumoniae (strain M129): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3