Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q329H3 (PHNN_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 55. 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:
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:SDY_4122
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP]
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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_0000412800

Regions

Nucleotide binding10 – 178ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q329H3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: FB8DD052F2E9B8BF

FASTA18520,689
        10         20         30         40         50         60 
MTGKLIWLMG PSGSGKDSLL AELRLREQTQ LLVAHRYITR DASAGSENHI ALSEQEFFTR 

        70         80         90        100        110        120 
AGQNLLALSW HANGLYYGVG VEIDLWLHAG FDVLVNGSRA HLPQARARYQ SALLPICLQV 

       130        140        150        160        170        180 
SPEILRQRLE NRGRENASEI NARLVRAARY TPQDCHTLNN DGSLCQSVDT LLTLIHQKEK 


HHACL 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sd197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000034 Genomic DNA. Translation: ABB64032.1.
RefSeqYP_405523.1. NC_007606.1.

3D structure databases

ProteinModelPortalQ329H3.
ModBaseSearch...

Protein-protein interaction databases

STRING300267.SDY_4122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB64032; ABB64032; SDY_4122.
GeneID3798889.
KEGGsdy:SDY_4122.
PATRIC18698983. VBIShiDys99784_4846.

Phylogenomic databases

eggNOGCOG3709.
HOGENOMHOG000037637.
KOK05774.
OMAKVINVTA.
ProtClustDBPRK10078.

Enzyme and pathway databases

BioCycSDYS300267:GJEW-4118-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_SHIDS
AccessionPrimary (citable) accession number: Q329H3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 55 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