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P0AG08 (RPE_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose-phosphate 3-epimerase
EC=5.1.3.1
Alternative name(s):
Pentose-5-phosphate 3-epimerase
Short name=PPE
R5P3E
Gene names
Name:rpe
Ordered Locus Names:c4156
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate By similarity.

Catalytic activity

D-ribulose 5-phosphate = D-xylulose 5-phosphate.

Cofactor

Binds 1 divalent metal cation per subunit. Active with Co2+, Mn2+ and Zn2+ By similarity.

Sequence similarities

Belongs to the ribulose-phosphate 3-epimerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandCobalt
Manganese
Metal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-phosphate 3-epimerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Ribulose-phosphate 3-epimerase
PRO_0000171570

Regions

Region144 – 1474Substrate binding By similarity
Region199 – 2002Substrate binding By similarity

Sites

Active site361Proton acceptor By similarity
Active site1771Proton donor By similarity
Metal binding341Divalent metal cation By similarity
Metal binding361Divalent metal cation By similarity
Metal binding681Divalent metal cation By similarity
Metal binding1771Divalent metal cation By similarity
Binding site91Substrate By similarity
Binding site681Substrate By similarity
Binding site1791Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AG08 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: DD678085698466FA

FASTA22524,554
        10         20         30         40         50         60 
MKQYLIAPSI LSADFARLGE DTAKALAAGA DVVHFDVMDN HYVPNLTIGP MVLKSLRNYG 

        70         80         90        100        110        120 
ITAPIDVHLM VKPVDRIVPD FAAAGASIIT FHPEASEHVD RTLQLIKENG CKAGLVFNPA 

       130        140        150        160        170        180 
TPLSYLDYVM DKLDVILLMS VNPGFGGQSF IPQTLDKLRE VRRRIDESGF DIRLEVDGGV 

       190        200        210        220 
KVNNIGEIAA AGADMFVAGS AIFDQPDYKK VIDEMRSELA KVSHE

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014075 Genomic DNA. Translation: AAN82594.1.
RefSeqNP_756020.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0AG08.
SMRP0AG08. Positions 6-222.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000044495; EBESCP00000042844; EBESCG00000043545.
GeneID1036696.
GenomeReviewsGene locus c4156 in contig AE014075_GR.
KEGGecc:c4156.
PATRIC18286058. VBIEscCol75197_3905.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009988.
HOGENOMHBG571751.
OMAHIDRTLQ.
PhylomeDBP0AG08.
ProtClustDBPRK05581.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR000056. Ribul_P_3_epim.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01783.
PANTHERPTHR11749. Ribul_P_3_epim. 1 hit.
PfamPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFPIRSF001461. RPE. 1 hit.
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR01163. Rpe. 1 hit.
PROSITEPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRPE_ECOL6
AccessionPrimary (citable) accession number: P0AG08
Secondary accession number(s): P32661
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 40 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

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