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P16687 (PHNI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI

Short name=RPnTP synthase subunit PhnI
EC=2.7.8.37
Alternative name(s):
Ribose 1-methylphosphonate 5-triphosphate synthase nucleosidase subunit
Gene names
Name:phnI
Ordered Locus Names:b4099, JW4060
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine. Ref.6

ATP + H2O = adenine + D-ribose 5-triphosphate. Ref.6

Subunit structure

Forms a complex with PhnG, PhnH, PhnJ and PhnK with the suggested composition PhnG4H2I2J2K. Ref.7

Miscellaneous

The sequence shown is that of strain K12.

Sequence similarities

Belongs to the PhnI family.

Biophysicochemical properties

Kinetic parameters:

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.

KM=64 µM for GTP (in the presence of PhnI alone) Ref.6

KM=95 µM for ATP (in the presence of PhnI alone)

KM=80 µM for GTP (in the presence of PhnI, PhnG, PhnH and PhnL)

KM=56 µM for ATP (in the presence of PhnI, PhnG, PhnH and PhnL)

Ontologies

Keywords
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processorganic phosphonate catabolic process

Inferred from mutant phenotype PubMed 8388873. Source: EcoCyc

   Molecular_functiontransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
PRO_0000058395

Natural variations

Natural variant2641G → D in strain: B.
Natural variant3511Q → K in strain: B.

Sequences

Sequence LengthMass (Da)Tools
P16687 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 9E974F01B85CCE81

FASTA35438,853
        10         20         30         40         50         60 
MYVAVKGGEK AIDAAHALQE SRRRGDTDLP ELSVAQIEQQ LNLAVDRVMT EGGIADRELA 

        70         80         90        100        110        120 
ALALKQASGD NVEAIFLLRA YRTTLAKLAV SEPLDTTGMR LERRISAVYK DIPGGQLLGP 

       130        140        150        160        170        180 
TYDYTHRLLD FTLLANGEAP TLTTADSEQQ PSPHVFSLLA RQGLAKFEED SGAQPDDITR 

       190        200        210        220        230        240 
TPPVYPCSRS SRLQQLMRGD EGYLLALAYS TQRGYGRNHP FAGEIRSGYI DVSIVPEELG 

       250        260        270        280        290        300 
FAVNVGELLM TECEMVNGFI DPPGEPPHFT RGYGLVFGMS ERKAMAMALV DRALQAPEYG 

       310        320        330        340        350 
EHATGPAQDE EFVLAHADNV EAAGFVSHLK LPHYVDFQAE LELLKRLQQE QNHG 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB65219.
RefSeqNP_418523.1. NC_000913.3.
YP_492243.1. NC_007779.1.

3D structure databases

ProteinModelPortalP16687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10488N.
IntActP16687. 2 interactions.
STRING511145.b4099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77060; AAC77060; b4099.
BAE78102; BAE78102; BAE78102.
GeneID12934387.
948605.
KEGGecj:Y75_p3987.
eco:b4099.
PATRIC32123757. VBIEscCol129921_4227.

Organism-specific databases

EchoBASEEB0712.
EcoGeneEG10718. phnI.

Phylogenomic databases

eggNOGCOG3626.
HOGENOMHOG000127007.
KOK06164.
OMAIANAHRL.
OrthoDBEOG609197.
PhylomeDBP16687.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP16687.

Family and domain databases

InterProIPR008773. PhnI.
[Graphical view]
PfamPF05861. PhnI. 1 hit.
[Graphical view]
PIRSFPIRSF007313. PhnI. 1 hit.
ProtoNetSearch...

Other

PROP16687.

Entry information

Entry namePHNI_ECOLI
AccessionPrimary (citable) accession number: P16687
Secondary accession number(s): Q2M6K4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

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