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Protein

Ribulose-phosphate 3-epimerase

Gene

Rpe

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Fe2+By similarity, Mn2+By similarity, Zn2+By similarity, Co2+By similarityNote: Binds 1 divalent metal cation per subunit. Active with Fe2+, and probably also with Mn2+, Zn2+ and Co2+.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10SubstrateBy similarity1
Metal bindingi35Divalent metal cationBy similarity1
Active sitei37Proton acceptorBy similarity1
Metal bindingi37Divalent metal cationBy similarity1
Metal bindingi70Divalent metal cationBy similarity1
Binding sitei70SubstrateBy similarity1
Active sitei175Proton donorBy similarity1
Metal bindingi175Divalent metal cationBy similarity1
Binding sitei177Substrate; via amide nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Cobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose-phosphate 3-epimerase (EC:5.1.3.1)
Alternative name(s):
Ribulose-5-phosphate-epimerase
Gene namesi
Name:Rpe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1913896. Rpe.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001715882 – 228Ribulose-phosphate 3-epimeraseAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8VEE0.
MaxQBiQ8VEE0.
PaxDbiQ8VEE0.
PRIDEiQ8VEE0.

PTM databases

PhosphoSitePlusiQ8VEE0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026005.
CleanExiMM_RPE.
ExpressionAtlasiQ8VEE0. baseline and differential.
GenevisibleiQ8VEE0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027157.

Structurei

3D structure databases

ProteinModelPortaliQ8VEE0.
SMRiQ8VEE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni146 – 149Substrate bindingBy similarity4
Regioni197 – 198Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3111. Eukaryota.
COG0036. LUCA.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
InParanoidiQ8VEE0.
KOiK01783.
PhylomeDBiQ8VEE0.
TreeFamiTF300157.

Family and domain databases

CDDicd00429. RPE. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VEE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG
60 70 80 90 100
HPVVESLRKQ LGQDPFFDMH MMVSRPEQWV KPMAVAGANQ YTFHLEATEN
110 120 130 140 150
PGALIKDIRE NGMKVGLAIK PGTTVEYLAP WANQIDMALV MTVEPGFGGQ
160 170 180 190 200
KFMEDMMPKV HWLRTQFPTL DIEVDGGVGP DTVQKCAEAG ANMIVSGSAI
210 220
MRSDDPRAVI NLLRNVCSEA AQKRSLDR
Length:228
Mass (Da):24,945
Last modified:March 1, 2002 - v1
Checksum:i81BBAF45F7EF48A8
GO

Sequence cautioni

The sequence BAC26287 differs from that shown.Curated
The sequence BAC26287 differs from that shown. Reason: Erroneous termination at position 229. Translated as stop.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007735 mRNA. No translation available.
AK017774 mRNA. Translation: BAB30922.2.
AK088152 mRNA. Translation: BAC40175.1.
AK029088 mRNA. Translation: BAC26287.1. Sequence problems.
BC019126 mRNA. Translation: AAH19126.1.
CCDSiCCDS15022.1.
RefSeqiNP_001297571.1. NM_001310642.1.
NP_001297572.1. NM_001310643.1.
NP_001297573.1. NM_001310644.1.
NP_079959.2. NM_025683.3.
UniGeneiMm.240912.

Genome annotation databases

EnsembliENSMUST00000027157; ENSMUSP00000027157; ENSMUSG00000026005.
GeneIDi66646.
KEGGimmu:66646.
UCSCiuc007bik.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007735 mRNA. No translation available.
AK017774 mRNA. Translation: BAB30922.2.
AK088152 mRNA. Translation: BAC40175.1.
AK029088 mRNA. Translation: BAC26287.1. Sequence problems.
BC019126 mRNA. Translation: AAH19126.1.
CCDSiCCDS15022.1.
RefSeqiNP_001297571.1. NM_001310642.1.
NP_001297572.1. NM_001310643.1.
NP_001297573.1. NM_001310644.1.
NP_079959.2. NM_025683.3.
UniGeneiMm.240912.

3D structure databases

ProteinModelPortaliQ8VEE0.
SMRiQ8VEE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027157.

PTM databases

PhosphoSitePlusiQ8VEE0.

Proteomic databases

EPDiQ8VEE0.
MaxQBiQ8VEE0.
PaxDbiQ8VEE0.
PRIDEiQ8VEE0.

Protocols and materials databases

DNASUi66646.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027157; ENSMUSP00000027157; ENSMUSG00000026005.
GeneIDi66646.
KEGGimmu:66646.
UCSCiuc007bik.1. mouse.

Organism-specific databases

CTDi6120.
MGIiMGI:1913896. Rpe.

Phylogenomic databases

eggNOGiKOG3111. Eukaryota.
COG0036. LUCA.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
InParanoidiQ8VEE0.
KOiK01783.
PhylomeDBiQ8VEE0.
TreeFamiTF300157.

Enzyme and pathway databases

ReactomeiR-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

PROiQ8VEE0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026005.
CleanExiMM_RPE.
ExpressionAtlasiQ8VEE0. baseline and differential.
GenevisibleiQ8VEE0. MM.

Family and domain databases

CDDicd00429. RPE. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPE_MOUSE
AccessioniPrimary (citable) accession number: Q8VEE0
Secondary accession number(s): Q8C130, Q9BSB5, Q9CQZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.