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P16687

- PHNI_ECOLI

UniProt

P16687 - PHNI_ECOLI

Protein

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI

Gene

phnI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively.1 Publication

    Catalytic activityi

    ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine.1 Publication
    ATP + H2O = adenine + D-ribose 5-triphosphate.1 Publication

    Kineticsi

    kcat is 1.4 sec(-1) for ATP hydrolysis in the presence of PhnI alone, and 20 sec(-1) for RPnTP synthesis from ATP in the presence of PhnI, PhnG, PhnH and PhnL.

    1. KM=64 µM for GTP (in the presence of PhnI alone)1 Publication
    2. KM=95 µM for ATP (in the presence of PhnI alone)1 Publication
    3. KM=80 µM for GTP (in the presence of PhnI, PhnG, PhnH and PhnL)1 Publication
    4. KM=56 µM for ATP (in the presence of PhnI, PhnG, PhnH and PhnL)1 Publication

    GO - Molecular functioni

    1. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. organic phosphonate catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10718-MONOMER.
    ECOL316407:JW4060-MONOMER.
    MetaCyc:EG10718-MONOMER.
    RETL1328306-WGS:GSTH-173-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI (EC:2.7.8.37)
    Short name:
    RPnTP synthase subunit PhnI
    Alternative name(s):
    Ribose 1-methylphosphonate 5-triphosphate synthase nucleosidase subunit
    Gene namesi
    Name:phnI
    Ordered Locus Names:b4099, JW4060
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10718. phnI.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnIPRO_0000058395Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP16687.

    Interactioni

    Subunit structurei

    Forms a complex with PhnG, PhnH, PhnJ and PhnK with the suggested composition PhnG4H2I2J2K.1 Publication

    Protein-protein interaction databases

    DIPiDIP-10488N.
    IntActiP16687. 2 interactions.
    STRINGi511145.b4099.

    Structurei

    3D structure databases

    ProteinModelPortaliP16687.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PhnI family.Curated

    Phylogenomic databases

    eggNOGiCOG3626.
    HOGENOMiHOG000127007.
    KOiK06164.
    OMAiIANAHRL.
    OrthoDBiEOG609197.
    PhylomeDBiP16687.

    Family and domain databases

    InterProiIPR008773. PhnI.
    [Graphical view]
    PfamiPF05861. PhnI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF007313. PhnI. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P16687-1 [UniParc]FASTAAdd to Basket

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    MYVAVKGGEK AIDAAHALQE SRRRGDTDLP ELSVAQIEQQ LNLAVDRVMT    50
    EGGIADRELA ALALKQASGD NVEAIFLLRA YRTTLAKLAV SEPLDTTGMR 100
    LERRISAVYK DIPGGQLLGP TYDYTHRLLD FTLLANGEAP TLTTADSEQQ 150
    PSPHVFSLLA RQGLAKFEED SGAQPDDITR TPPVYPCSRS SRLQQLMRGD 200
    EGYLLALAYS TQRGYGRNHP FAGEIRSGYI DVSIVPEELG FAVNVGELLM 250
    TECEMVNGFI DPPGEPPHFT RGYGLVFGMS ERKAMAMALV DRALQAPEYG 300
    EHATGPAQDE EFVLAHADNV EAAGFVSHLK LPHYVDFQAE LELLKRLQQE 350
    QNHG 354
    Length:354
    Mass (Da):38,853
    Last modified:November 1, 1991 - v2
    Checksum:i9E974F01B85CCE81
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti264 – 2641G → D in strain: B.
    Natural varianti351 – 3511Q → K in strain: B.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05260 Genomic DNA. Translation: AAA24347.1.
    D90227 Genomic DNA. Translation: BAA14269.1.
    U14003 Genomic DNA. Translation: AAA96998.1.
    U00096 Genomic DNA. Translation: AAC77060.1.
    AP009048 Genomic DNA. Translation: BAE78102.1.
    PIRiB65219.
    RefSeqiNP_418523.1. NC_000913.3.
    YP_492243.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77060; AAC77060; b4099.
    BAE78102; BAE78102; BAE78102.
    GeneIDi12934387.
    948605.
    KEGGiecj:Y75_p3987.
    eco:b4099.
    PATRICi32123757. VBIEscCol129921_4227.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05260 Genomic DNA. Translation: AAA24347.1 .
    D90227 Genomic DNA. Translation: BAA14269.1 .
    U14003 Genomic DNA. Translation: AAA96998.1 .
    U00096 Genomic DNA. Translation: AAC77060.1 .
    AP009048 Genomic DNA. Translation: BAE78102.1 .
    PIRi B65219.
    RefSeqi NP_418523.1. NC_000913.3.
    YP_492243.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P16687.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10488N.
    IntActi P16687. 2 interactions.
    STRINGi 511145.b4099.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77060 ; AAC77060 ; b4099 .
    BAE78102 ; BAE78102 ; BAE78102 .
    GeneIDi 12934387.
    948605.
    KEGGi ecj:Y75_p3987.
    eco:b4099.
    PATRICi 32123757. VBIEscCol129921_4227.

    Organism-specific databases

    EchoBASEi EB0712.
    EcoGenei EG10718. phnI.

    Phylogenomic databases

    eggNOGi COG3626.
    HOGENOMi HOG000127007.
    KOi K06164.
    OMAi IANAHRL.
    OrthoDBi EOG609197.
    PhylomeDBi P16687.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10718-MONOMER.
    ECOL316407:JW4060-MONOMER.
    MetaCyc:EG10718-MONOMER.
    RETL1328306-WGS:GSTH-173-MONOMER.

    Miscellaneous databases

    PROi P16687.

    Gene expression databases

    Genevestigatori P16687.

    Family and domain databases

    InterProi IPR008773. PhnI.
    [Graphical view ]
    Pfami PF05861. PhnI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF007313. PhnI. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B."
      Chen C.-M., Ye Q.-Z., Zhu Z., Wanner B.L., Walsh C.T.
      J. Biol. Chem. 265:4461-4471(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B.
    2. "Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12."
      Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A.
      J. Bacteriol. 173:2665-2672(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Intermediates in the transformation of phosphonates to phosphate by bacteria."
      Kamat S.S., Williams H.J., Raushel F.M.
      Nature 480:570-573(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway."
      Jochimsen B., Lolle S., McSorley F.R., Nabi M., Stougaard J., Zechel D.L., Hove-Jensen B.
      Proc. Natl. Acad. Sci. U.S.A. 108:11393-11398(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
      Strain: K12.

    Entry informationi

    Entry nameiPHNI_ECOLI
    AccessioniPrimary (citable) accession number: P16687
    Secondary accession number(s): Q2M6K4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 100 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
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3