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Protein

Ribulose-phosphate 3-epimerase

Gene

rpe

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101SubstrateUniRule annotation
Metal bindingi35 – 351Divalent metal cationUniRule annotation
Active sitei37 – 371Proton acceptorUniRule annotation
Metal bindingi37 – 371Divalent metal cationUniRule annotation
Metal bindingi70 – 701Divalent metal cationUniRule annotation
Binding sitei70 – 701SubstrateUniRule annotation
Active sitei175 – 1751Proton donorUniRule annotation
Metal bindingi175 – 1751Divalent metal cationUniRule annotation
Binding sitei177 – 1771Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotation

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Keywords - Ligandi

CobaltUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation, ZincUniRule annotation

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose-phosphate 3-epimeraseUniRule annotation (EC:5.1.3.1UniRule annotation)
Gene namesi
Name:rpeImported
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)Imported
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 9

Organism-specific databases

ZFINiZDB-GENE-030131-6837. rpe.

Expressioni

Gene expression databases

ExpressionAtlasiQ6PBW9. differential.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000023863.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni146 – 1494Substrate bindingUniRule annotation
Regioni197 – 1982Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ribulose-phosphate 3-epimerase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3111. Eukaryota.
COG0036. LUCA.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
KOiK01783.
OMAiKTIDVCA.
OrthoDBiEOG789CC1.
PhylomeDBiQ6PBW9.
TreeFamiTF300157.

Family and domain databases

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.

Q6PBW9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYTAKIGPS ILSSDLSQLG RECERMMECG ADYLHLDVMD GHFVPNITFG
60 70 80 90 100
HPMVECLRSC IGPDPFFDMH MMVSRPEQWV KPMAAAGANQ YTFHLEATSN
110 120 130 140 150
PGNLIKEIRE SGMKVGLAIK PGTTVEELAP WAGQIDMALV MTVEPGFGGQ
160 170 180 190 200
KFMEDMMPKV SWLRGQFPSL DIEVDGGVGP DSIHRCAEAG ANMIVSGSAV
210 220
VSSDDPRSVI ALLKNVVMEA IQKRSLDR
Length:228
Mass (Da):24,846
Last modified:July 5, 2004 - v1
Checksum:i790B6019D4D2D217
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR545476 Genomic DNA. No translation available.
BC059555 mRNA. Translation: AAH59555.1.
RefSeqiNP_001230353.1. NM_001243424.1.
UniGeneiDr.75331.

Genome annotation databases

EnsembliENSDART00000021218; ENSDARP00000023863; ENSDARG00000005251.
GeneIDi334897.
KEGGidre:334897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR545476 Genomic DNA. No translation available.
BC059555 mRNA. Translation: AAH59555.1.
RefSeqiNP_001230353.1. NM_001243424.1.
UniGeneiDr.75331.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000023863.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000021218; ENSDARP00000023863; ENSDARG00000005251.
GeneIDi334897.
KEGGidre:334897.

Organism-specific databases

CTDi6120.
ZFINiZDB-GENE-030131-6837. rpe.

Phylogenomic databases

eggNOGiKOG3111. Eukaryota.
COG0036. LUCA.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
KOiK01783.
OMAiKTIDVCA.
OrthoDBiEOG789CC1.
PhylomeDBiQ6PBW9.
TreeFamiTF300157.

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasiQ6PBW9. differential.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Wild-typeImported.
    Tissue: EyeImported.
  2. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: TuebingenImported.
  3. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TuebingenImported.

Entry informationi

Entry nameiQ6PBW9_DANRE
AccessioniPrimary (citable) accession number: Q6PBW9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.