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Q5NFM5 (RPIA_FRATT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-5-phosphate isomerase A

EC=5.3.1.6
Alternative name(s):
Phosphoriboisomerase A
Short name=PRI
Gene names
Name:rpiA
Ordered Locus Names:FTT_1208
OrganismFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) [Reference proteome] [HAMAP]
Taxonomic identifier177416 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate By similarity. HAMAP-Rule MF_00170

Catalytic activity

D-ribose 5-phosphate = D-ribulose 5-phosphate. HAMAP-Rule MF_00170

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. HAMAP-Rule MF_00170

Subunit structure

Homodimer and homotetramer. Ref.2 Ref.3

Sequence similarities

Belongs to the ribose 5-phosphate isomerase family.

Ontologies

Keywords
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt, non-oxidative branch

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionribose-5-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224Ribose-5-phosphate isomerase A HAMAP-Rule MF_00170
PRO_0000158419

Regions

Region34 – 374Substrate binding Probable
Region87 – 904Substrate binding By similarity
Region100 – 1034Substrate binding Probable

Sites

Active site1091Proton acceptor Probable
Binding site1271Substrate

Secondary structure

........................................... 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5NFM5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 46ACC58D7487CC2B

FASTA22424,466
        10         20         30         40         50         60 
MFFNKKNNQD ELKKLAATEA AKSITTEITL GVGTGSTVGF LIEELVNYRD KIKTVVSSSE 

        70         80         90        100        110        120 
DSTRKLKALG FDVVDLNYAG EIDLYIDGAD ECNNHKELIK GGGAALTREK ICVAAAKKFI 

       130        140        150        160        170        180 
CIIDESKKVN TLGNFPLPIE VIPMARSYIA RQIVKLGGQP VYREQTITDN GNVILDVYNL 

       190        200        210        220 
KIDNPLKLET ELNQITGVVT NGIFALKPAD TVIMATKDSN IVVL 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Francisella tularensis, the causative agent of tularemia."
Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H., Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D., Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S., Sjoestedt A. expand/collapse author list , Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W., Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.
Nat. Genet. 37:153-159(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCHU S4 / Schu 4.
[2]"Crystal structure of ribose-5-isomerase A."
Center for Structural Genomics of Infectious Diseases (CSGID)
Orlikowska M., Rostankowski R., Nakka C., Hattne J., Grimshaw S., Borek D., Otwinowski Z.
Submitted (DEC-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.
[3]"Structural and biophysical studies of Ribose-5-Phosphate Isomerase A from Francisella tularensis."
Center for Structural Genomics of Infectious Diseases (CSGID)
Rostankowski R., Orlikowska M., Nakka C., Grimshaw S., Borek D., Otwinowski Z.
Submitted (JAN-2013) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ749949 Genomic DNA. Translation: CAG45841.1.
RefSeqYP_170167.1. NC_006570.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KWMX-ray2.32A/B/C/D1-224[»]
4IO1X-ray1.65A/B1-224[»]
ProteinModelPortalQ5NFM5.
SMRQ5NFM5. Positions 8-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177416.FTT_1208.

Protocols and materials databases

DNASU3192024.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG45841; CAG45841; FTT_1208.
GeneID3192024.
KEGGftu:FTT_1208.

Phylogenomic databases

eggNOGCOG0120.
HOGENOMHOG000276368.
KOK01807.
OMAMDQLEMK.
OrthoDBEOG67MF61.

Enzyme and pathway databases

BioCycFTUL177416:GNBP-1226-MONOMER.
UniPathwayUPA00115; UER00412.

Family and domain databases

HAMAPMF_00170. Rib_5P_isom_A.
InterProIPR004788. Ribose5P_isomerase_typA.
IPR020672. Ribose5P_isomerase_typA_subgr.
[Graphical view]
PANTHERPTHR11934. PTHR11934. 1 hit.
PfamPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsTIGR00021. rpiA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRPIA_FRATT
AccessionPrimary (citable) accession number: Q5NFM5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 60 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways