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P0AG07 (RPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:dod, yhfD
Ordered Locus Names:b3386, JW3349
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dnaNP0A9882EBI-546020,EBI-542385

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Ribulose-phosphate 3-epimerase
PRO_0000171568

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

Experimental info

Sequence conflict203 – 22523FDQPD…KVSHE → LTSQTTKKSTMKCAVNWQR in CAA79663. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0AG07 [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

« Hide 'large scale' references
[1]"Characterization of three genes in the dam-containing operon of Escherichia coli."
Lyngstadaas A., Lobner-Olesen A., Boye E.
Mol. Gen. Genet. 247:546-554(1995) [PubMed: 7603433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z19601 Genomic DNA. Translation: CAA79663.1.
U18997 Genomic DNA. Translation: AAA58183.1.
U00096 Genomic DNA. Translation: AAC76411.1.
AP009048 Genomic DNA. Translation: BAE77905.1.
PIRE65133.
RefSeqNP_417845.1. NC_000913.2.

3D structure databases

ProteinModelPortalP0AG07.
SMRP0AG07. Positions 6-222.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47869N.
IntActP0AG07. 26 interactions.
MINTMINT-1228320.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000942; EBESCP00000000942; EBESCG00000000777.
EBESCT00000000943; EBESCP00000000943; EBESCG00000000777.
EBESCT00000000944; EBESCP00000000944; EBESCG00000000777.
EBESCT00000000945; EBESCP00000000945; EBESCG00000000777.
EBESCT00000000946; EBESCP00000000946; EBESCG00000000777.
EBESCT00000000947; EBESCP00000000947; EBESCG00000000777.
EBESCT00000014716; EBESCP00000014007; EBESCG00000013777.
GeneID947896.
GenomeReviewsGene locus JW3349 in contig AP009048_GR.
Gene locus b3386 in contig U00096_GR.
KEGGecj:JW3349.
eco:b3386.
PATRIC32122204. VBIEscCol129921_3479.

Organism-specific databases

EchoBASEEB1903.
EcoGeneEG11960. rpe.

Phylogenomic databases

eggNOGCOG0036.
GeneTreeEBGT00050000009988.
HOGENOMHBG571751.
OMAHIDRTLQ.
PhylomeDBP0AG07.
ProtClustDBPRK05581.

Enzyme and pathway databases

BioCycEcoCyc:RIBULP3EPIM-MONOMER.
MetaCyc:RIBULP3EPIM-MONOMER.

Gene expression databases

GenevestigatorP0AG07.

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_ECOLI
AccessionPrimary (citable) accession number: P0AG07
Secondary accession number(s): P32661, Q2M751
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families