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Protein

Ribose 1,5-bisphosphate phosphokinase PhnN

Gene

phnN

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

Functioni

Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). Accepts ATP but not GTP as a phosphoryl donor, and uses ribose 1,5-bisphosphate but not ribose, ribose 1-phosphate, or ribose 5-phosphate as a phosphoryl acceptor.2 Publications

Catalytic activityi

ATP + alpha-D-ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Phosphopentomutase (deoB)
  2. no protein annotated in this organism
  3. Ribose 1,5-bisphosphate phosphokinase PhnN (phnN)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ribose 1,5-bisphosphate phosphokinase activity Source: UniProtKB

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: UniProtKB
  • organic phosphonate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10723-MONOMER.
ECOL316407:JW4055-MONOMER.
MetaCyc:EG10723-MONOMER.
UniPathwayiUPA00087; UER00175.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose 1,5-bisphosphate phosphokinase PhnN (EC:2.7.4.23)
Alternative name(s):
Ribose 1,5-bisphosphokinase
Gene namesi
Name:phnN
Ordered Locus Names:b4094, JW4055
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10723. phnN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Ribose 1,5-bisphosphate phosphokinase PhnNPRO_0000058400Add
BLAST

Proteomic databases

PaxDbiP16690.
PRIDEiP16690.

Interactioni

Protein-protein interaction databases

IntActiP16690. 33 interactions.
STRINGi511145.b4094.

Structurei

3D structure databases

ProteinModelPortaliP16690.
SMRiP16690. Positions 2-28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribose 1,5-bisphosphokinase family.Curated

Phylogenomic databases

eggNOGiENOG4105MFQ. Bacteria.
COG3709. LUCA.
HOGENOMiHOG000037637.
InParanoidiP16690.
KOiK05774.
OMAiMARLIWL.
OrthoDBiEOG67MF7F.
PhylomeDBiP16690.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00836. PhnN.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR012699. PhnN.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02322. phosphon_PhnN. 1 hit.

Sequencei

Sequence statusi: Complete.

P16690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMGKLIWLMG PSGSGKDSLL AELRLREQTQ LLVAHRYITR DASAGSENHI
60 70 80 90 100
ALSEQEFFTR AGQNLLALSW HANGLYYGVG VEIDLWLHAG FDVLVNGSRA
110 120 130 140 150
HLPQARARYQ SALLPVCLQV SPEILRQRLE NRGRENASEI NARLARAARY
160 170 180
TPQDCHTLNN DGSLRQSVDT LLTLIHQKEK HHACL
Length:185
Mass (Da):20,730
Last modified:August 1, 1990 - v1
Checksum:i399ADE57C7975325
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24353.1.
D90227 Genomic DNA. Translation: BAA14274.1.
U14003 Genomic DNA. Translation: AAA96993.1.
U00096 Genomic DNA. Translation: AAC77055.1.
AP009048 Genomic DNA. Translation: BAE78097.1.
PIRiF35719.
RefSeqiNP_418518.1. NC_000913.3.
WP_000971886.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77055; AAC77055; b4094.
BAE78097; BAE78097; BAE78097.
GeneIDi948608.
KEGGiecj:JW4055.
eco:b4094.
PATRICi32123747. VBIEscCol129921_4222.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24353.1.
D90227 Genomic DNA. Translation: BAA14274.1.
U14003 Genomic DNA. Translation: AAA96993.1.
U00096 Genomic DNA. Translation: AAC77055.1.
AP009048 Genomic DNA. Translation: BAE78097.1.
PIRiF35719.
RefSeqiNP_418518.1. NC_000913.3.
WP_000971886.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP16690.
SMRiP16690. Positions 2-28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16690. 33 interactions.
STRINGi511145.b4094.

Proteomic databases

PaxDbiP16690.
PRIDEiP16690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77055; AAC77055; b4094.
BAE78097; BAE78097; BAE78097.
GeneIDi948608.
KEGGiecj:JW4055.
eco:b4094.
PATRICi32123747. VBIEscCol129921_4222.

Organism-specific databases

EchoBASEiEB0717.
EcoGeneiEG10723. phnN.

Phylogenomic databases

eggNOGiENOG4105MFQ. Bacteria.
COG3709. LUCA.
HOGENOMiHOG000037637.
InParanoidiP16690.
KOiK05774.
OMAiMARLIWL.
OrthoDBiEOG67MF7F.
PhylomeDBiP16690.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00175.
BioCyciEcoCyc:EG10723-MONOMER.
ECOL316407:JW4055-MONOMER.
MetaCyc:EG10723-MONOMER.

Miscellaneous databases

PROiP16690.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00836. PhnN.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR012699. PhnN.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02322. phosphon_PhnN. 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. "Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways."
    Hove-Jensen B., Rosenkrantz T.J., Haldimann A., Wanner B.L.
    J. Bacteriol. 185:2793-2801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RIBOSE 1,5-BISPHOSPHOKINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  7. "A fluorescent substrate for carbon-phosphorus lyase: towards the pathway for organophosphonate metabolism in bacteria."
    He S.M., Luo Y., Hove-Jensen B., Zechel D.L.
    Bioorg. Med. Chem. Lett. 19:5954-5957(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE ORGANOPHOSPHONATE METABOLISM.
  8. "Accumulation of intermediates of the carbon-phosphorus lyase pathway for phosphonate degradation in phn mutants of Escherichia coli."
    Hove-Jensen B., Rosenkrantz T.J., Zechel D.L., Willemoes M.
    J. Bacteriol. 192:370-374(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiPHNN_ECOLI
AccessioniPrimary (citable) accession number: P16690
Secondary accession number(s): Q2M6K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 6, 2016
This is version 119 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.