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B5QXJ0 (RPIA_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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-5-phosphate isomerase A

EC=5.3.1.6
Alternative name(s):
Phosphoriboisomerase A
Short name=PRI
Gene names
Name:rpiA
Ordered Locus Names:SEN2906
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00170

Sequence similarities

Belongs to the ribose 5-phosphate isomerase family.

Ontologies

Keywords
   Molecular functionIsomerase
   Technical termComplete 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 – 219219Ribose-5-phosphate isomerase A HAMAP-Rule MF_00170
PRO_1000097690

Regions

Region28 – 314Substrate binding By similarity
Region81 – 844Substrate binding By similarity
Region94 – 974Substrate binding By similarity

Sites

Active site1031Proton acceptor By similarity
Binding site1211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B5QXJ0 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: FEA022A02971BF3B

FASTA21922,895
        10         20         30         40         50         60 
MTQDELKKAV GWAALQYVQP GTIVGVGTGS TAAHFIDALG TMKGQIEGAV SSSDASTEKL 

        70         80         90        100        110        120 
KGLGIHVFDL NEVDSLGIYV DGADEINGHM QMIKGGGAAL TREKIIASVA EKFICIADAS 

       130        140        150        160        170        180 
KQVDILGKFP LPVEVIPMAR SAVARQLVKL GGRPEYRQNV VTDNGNVILD VYGMEILDPI 

       190        200        210 
ALENAINAIP GVVTVGLFAN RGADVALIGT PDGVKTIVK 

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR34484.1.
RefSeqYP_002244977.1. NC_011294.1.

3D structure databases

ProteinModelPortalB5QXJ0.
SMRB5QXJ0. Positions 1-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN2906.

Proteomic databases

PRIDEB5QXJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC32336409. VBISalEnt14964_2961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0120.
HOGENOMHOG000276368.
OMAGACHVQE.
OrthoDBEOG67MF61.
ProtClustDBPRK00702.

Enzyme and pathway databases

BioCycSENT550537:GJFI-2947-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_SALEP
AccessionPrimary (citable) accession number: B5QXJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: February 19, 2014
This is version 36 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

PATHWAY comments

Index of metabolic and biosynthesis pathways