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Protein

Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

Gene

phnM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of alpha-D-ribose 1-methylphosphonate triphosphate (RPnTP) to form alpha-D-ribose 1-methylphosphonate phosphate (PRPn) and diphosphate.1 Publication

Catalytic activityi

Alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate.1 Publication

Kineticsi

  1. KM=56 µM for alpha-D-ribose 1-methylphosphonate 5-triphosphate1 Publication
  2. KM=98 µM for D-ribose-5-triphosphate1 Publication
  3. KM=200 µM for D-ribose-5-diphosphate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • organic phosphonate catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10722-MONOMER.
    ECOL316407:JW4056-MONOMER.
    MetaCyc:EG10722-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase (EC:3.6.1.63)
    Short name:
    RPnTP diphosphatase
    Gene namesi
    Name:phnM
    Ordered Locus Names:b4095, JW4056
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10722. phnM.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000583991 – 378Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphataseAdd BLAST378

    Proteomic databases

    PaxDbiP16689.
    PRIDEiP16689.

    Interactioni

    Protein-protein interaction databases

    BioGridi4262021. 7 interactors.
    STRINGi511145.b4095.

    Structurei

    3D structure databases

    ProteinModelPortaliP16689.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiENOG4105FD8. Bacteria.
    COG3454. LUCA.
    HOGENOMiHOG000126996.
    InParanoidiP16689.
    KOiK06162.
    OMAiWSQPNRQ.
    PhylomeDBiP16689.

    Family and domain databases

    CDDicd01306. PhnM. 1 hit.
    Gene3Di2.30.40.10. 1 hit.
    InterProiIPR013108. Amidohydro_3.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR032466. Metal_Hydrolase.
    IPR012696. PhnM.
    [Graphical view]
    PfamiPF07969. Amidohydro_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038971. PhnM. 1 hit.
    SUPFAMiSSF51338. SSF51338. 2 hits.
    SSF51556. SSF51556. 1 hit.
    TIGRFAMsiTIGR02318. phosphono_phnM. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P16689-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIINNVKLVL ENEVVSGSLE VQNGEIRAFA ESQSRLPEAM DGEGGWLLPG
    60 70 80 90 100
    LIELHTDNLD KFFTPRPKVD WPAHSAMSSH DALMVASGIT TVLDAVAIGD
    110 120 130 140 150
    VRDGGDRLEN LEKMINAIEE TQKRGVNRAE HRLHLRCELP HHTTLPLFEK
    160 170 180 190 200
    LVQREPVTLV SLMDHSPGQR QFANREKYRE YYQGKYSLTD AQMQQYEEEQ
    210 220 230 240 250
    LALAARWSQP NRESIAALCR ARKIALASHD DATHAHVAES HQLGSVIAEF
    260 270 280 290 300
    PTTFEAAEAS RKHGMNVLMG APNIVRGGSH SGNVAASELA QLGLLDILSS
    310 320 330 340 350
    DYYPASLLDA AFRVADDQSN RFTLPQAVKL VTKNPAQALN LQDRGVIGEG
    360 370
    KRADLVLAHR KDNHIHIDHV WRQGKRVF
    Length:378
    Mass (Da):42,010
    Last modified:November 1, 1991 - v2
    Checksum:i28CC9C5C77EAD37D
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti318Q → E in strain: B. 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05260 Genomic DNA. Translation: AAA24352.1.
    D90227 Genomic DNA. Translation: BAA14273.1.
    U14003 Genomic DNA. Translation: AAA96994.1.
    U00096 Genomic DNA. Translation: AAC77056.1.
    AP009048 Genomic DNA. Translation: BAE78098.1.
    PIRiS56323.
    RefSeqiNP_418519.1. NC_000913.3.
    WP_000586325.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77056; AAC77056; b4095.
    BAE78098; BAE78098; BAE78098.
    GeneIDi948613.
    KEGGiecj:JW4056.
    eco:b4095.
    PATRICi32123749. VBIEscCol129921_4223.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05260 Genomic DNA. Translation: AAA24352.1.
    D90227 Genomic DNA. Translation: BAA14273.1.
    U14003 Genomic DNA. Translation: AAA96994.1.
    U00096 Genomic DNA. Translation: AAC77056.1.
    AP009048 Genomic DNA. Translation: BAE78098.1.
    PIRiS56323.
    RefSeqiNP_418519.1. NC_000913.3.
    WP_000586325.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP16689.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262021. 7 interactors.
    STRINGi511145.b4095.

    Proteomic databases

    PaxDbiP16689.
    PRIDEiP16689.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77056; AAC77056; b4095.
    BAE78098; BAE78098; BAE78098.
    GeneIDi948613.
    KEGGiecj:JW4056.
    eco:b4095.
    PATRICi32123749. VBIEscCol129921_4223.

    Organism-specific databases

    EchoBASEiEB0716.
    EcoGeneiEG10722. phnM.

    Phylogenomic databases

    eggNOGiENOG4105FD8. Bacteria.
    COG3454. LUCA.
    HOGENOMiHOG000126996.
    InParanoidiP16689.
    KOiK06162.
    OMAiWSQPNRQ.
    PhylomeDBiP16689.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10722-MONOMER.
    ECOL316407:JW4056-MONOMER.
    MetaCyc:EG10722-MONOMER.

    Miscellaneous databases

    PROiP16689.

    Family and domain databases

    CDDicd01306. PhnM. 1 hit.
    Gene3Di2.30.40.10. 1 hit.
    InterProiIPR013108. Amidohydro_3.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR032466. Metal_Hydrolase.
    IPR012696. PhnM.
    [Graphical view]
    PfamiPF07969. Amidohydro_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038971. PhnM. 1 hit.
    SUPFAMiSSF51338. SSF51338. 2 hits.
    SSF51556. SSF51556. 1 hit.
    TIGRFAMsiTIGR02318. phosphono_phnM. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPHNM_ECOLI
    AccessioniPrimary (citable) accession number: P16689
    Secondary accession number(s): Q2M6K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: November 1, 1991
    Last modified: November 2, 2016
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The sequence shown is that of strain K12.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.