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Q7NWY0 (PHNN_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribose 1,5-bisphosphate phosphokinase PhnN

EC=2.7.4.23
Alternative name(s):
Ribose 1,5-bisphosphokinase
Gene names
Name:phnN
Ordered Locus Names:CV_1849
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP) By similarity. HAMAP-Rule MF_00836

Catalytic activity

ATP + alpha-D-ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00836

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3. HAMAP-Rule MF_00836

Sequence similarities

Belongs to the ribose 1,5-bisphosphokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Ribose 1,5-bisphosphate phosphokinase PhnN HAMAP-Rule MF_00836
PRO_0000412778

Regions

Nucleotide binding13 – 208ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NWY0 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 62F3E111C524A1AD

FASTA18520,091
        10         20         30         40         50         60 
MADKTGTLWY VMGPSGAGKD SLLAYARQRL PGGVMFAHRY ITRPADAGGE NHVALSREEF 

        70         80         90        100        110        120 
DAREAGGCFA LVWRRHGLAY GLGVETELWL GQGMDVVVNG SRSSLPLAMA RFPTLRPLWI 

       130        140        150        160        170        180 
TASPEVLAVR LRQRARECGE VIERRLAEAA SFAPPAGCEV LVNDGALAQA GDTLLRWLRG 


GRRVC 

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ59523.1.
RefSeqNP_901519.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NWY0.
ModBaseSearch...

Protein-protein interaction databases

STRING243365.CV_1849.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ59523; AAQ59523; CV_1849.
GeneID2549109.
KEGGcvi:CV_1849.
PATRIC21438504. VBIChrVio67196_1812.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000037637.
KOK05774.
OMAKVINVTA.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-1848-MONOMER.
UniPathwayUPA00087; UER00175.

Family and domain databases

HAMAPMF_00836. PhnN.
InterProIPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR012699. PhnN.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
[Graphical view]
TIGRFAMsTIGR02322. phosphon_PhnN. 1 hit.
PROSITEPS50052. GUANYLATE_KINASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHNN_CHRVO
AccessionPrimary (citable) accession number: Q7NWY0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: December 15, 2003
Last modified: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families