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Protein

Ribulose-phosphate 3-epimerase

Gene

cbbE

Organism
Rhodospirillum rubrum
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

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

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10SubstrateBy similarity1
Metal bindingi35Divalent metal cationBy similarity1
Active sitei37Proton acceptorBy similarity1
Metal bindingi37Divalent metal cationBy similarity1
Metal bindingi68Divalent metal cationBy similarity1
Binding sitei68SubstrateBy similarity1
Active sitei175Proton donorBy similarity1
Metal bindingi175Divalent metal cationBy similarity1
Binding sitei177Substrate; via amide nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processCalvin cycle, Carbohydrate metabolism
LigandCobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose-phosphate 3-epimerase (EC:5.1.3.1)
Alternative name(s):
Pentose-5-phosphate 3-epimerase
Short name:
PPE
R5P3E
Gene namesi
Name:cbbE
OrganismiRhodospirillum rubrum
Taxonomic identifieri1085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001715591 – 225Ribulose-phosphate 3-epimeraseAdd BLAST225

Proteomic databases

PRIDEiP51013.

Structurei

3D structure databases

ProteinModelPortaliP51013.
SMRiP51013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 147Substrate bindingBy similarity4

Sequence similaritiesi

Family and domain databases

CDDicd00429. RPE. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiView protein in Pfam
PF00834. Ribul_P_3_epim. 1 hit.
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiView protein in PROSITE
PS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P51013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRAIRIAPS LLSADFAISR PRCPSDGRTG ADILHFDVMD NHYVPNLTVG
60 70 80 90 100
PLVCAALRPH TSLPIDVHLM TRPVDPLIDS FAEAGADMIT FHPEASDHVH
110 120 130 140 150
RSVQMIRKRG LKAGVALNPA SPLSLLDHIL EDLDLVLIMS VNPGFGGQSF
160 170 180 190 200
IPSALPKIAA LANGRRRACR GDRVDGGVNP ADARALARPG ADILVRLAIF
210 220
GASDRAKAIA SIRGAAESGL GQEAA
Length:225
Mass (Da):23,765
Last modified:July 15, 1998 - v2
Checksum:i143D9631241F0E3C
GO

Sequence cautioni

The sequence AAB27778 differs from that shown. Reason: Frameshift at position 191.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S64484 Genomic DNA. Translation: AAB27778.1. Frameshift.
PIRiA53305.

Similar proteinsi

Entry informationi

Entry nameiRPE_RHORU
AccessioniPrimary (citable) accession number: P51013
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: March 15, 2017
This is version 68 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families