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Protein

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

Gene

phnI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: 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.
InParanoidiP16687.
KOiK06164.
OMAiLTECQMV.
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

« Hide

        10         20         30         40         50
MYVAVKGGEK AIDAAHALQE SRRRGDTDLP ELSVAQIEQQ LNLAVDRVMT
60 70 80 90 100
EGGIADRELA ALALKQASGD NVEAIFLLRA YRTTLAKLAV SEPLDTTGMR
110 120 130 140 150
LERRISAVYK DIPGGQLLGP TYDYTHRLLD FTLLANGEAP TLTTADSEQQ
160 170 180 190 200
PSPHVFSLLA RQGLAKFEED SGAQPDDITR TPPVYPCSRS SRLQQLMRGD
210 220 230 240 250
EGYLLALAYS TQRGYGRNHP FAGEIRSGYI DVSIVPEELG FAVNVGELLM
260 270 280 290 300
TECEMVNGFI DPPGEPPHFT RGYGLVFGMS ERKAMAMALV DRALQAPEYG
310 320 330 340 350
EHATGPAQDE EFVLAHADNV EAAGFVSHLK LPHYVDFQAE LELLKRLQQE

QNHG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP16687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0712.
EcoGeneiEG10718. phnI.

Phylogenomic databases

eggNOGiCOG3626.
HOGENOMiHOG000127007.
InParanoidiP16687.
KOiK06164.
OMAiLTECQMV.
OrthoDBiEOG609197.
PhylomeDBiP16687.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP16687.

Gene expression databases

GenevestigatoriP16687.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 102 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

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 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.