Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40117 (RPEC_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose-phosphate 3-epimerase, chromosomal

EC=5.1.3.1
Alternative name(s):
Pentose-5-phosphate 3-epimerase
Short name=PPE
R5P3E
Gene names
Name:cbbEC
Synonyms:cbbE2, cfxE
Ordered Locus Names:H16_B1391
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length241 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+, Fe2+, Mn2+ and Zn2+ By similarity.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Sequence similarities

Belongs to the ribulose-phosphate 3-epimerase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Ribulose-phosphate 3-epimerase, chromosomal
PRO_0000171556

Regions

Region155 – 1584Substrate binding By similarity
Region214 – 2152Substrate binding By similarity

Sites

Active site481Proton acceptor By similarity
Active site1921Proton donor By similarity
Metal binding461Divalent metal cation By similarity
Metal binding481Divalent metal cation By similarity
Metal binding791Divalent metal cation By similarity
Metal binding1921Divalent metal cation By similarity
Binding site211Substrate By similarity
Binding site791Substrate By similarity
Binding site1941Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P40117 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 9B6CC244FD1215CC

FASTA24125,501
        10         20         30         40         50         60 
MHATELNTGH GSQRAIRLAP SILSADFARL GEEVCAIEAG GADLVHFDVM DNHYVPNLTI 

        70         80         90        100        110        120 
GPLVCEAIRP LVSIPIDVHL MVEPVDALIP LFAKAGANII SFHPEASRHV DRTIGLIRDH 

       130        140        150        160        170        180 
GCKAGLVLNP ATPLGWLDHT LDQLDLVLLM SVNPGFGGQA FIPGVLDKVR QARARIDRQV 

       190        200        210        220        230        240 
DAGGRPVWLE IDGGVKADNI AAIARAGADT FVAGSAVFGA PDADGGYSSI LYRLREAATV 


T 

« Hide

References

« Hide 'large scale' references
[1]"The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus."
Kusian B., Yoo J.-G., Bednarski R., Bowien B.
J. Bacteriol. 174:7337-7344(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64173 Genomic DNA. Translation: AAA21962.1.
AM260480 Genomic DNA. Translation: CAJ96180.1.
PIRC47019.
RefSeqYP_840910.1. NC_008314.1.

3D structure databases

ProteinModelPortalP40117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B1391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ96180; CAJ96180; H16_B1391.
GeneID4456350.
KEGGreh:H16_B1391.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0036.
HOGENOMHOG000259347.
KOK01783.
OMARISFHVE.
OrthoDBEOG67HK17.
ProtClustDBCLSK648281.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-5096-MONOMER.
UniPathwayUPA00116.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERPTHR11749. PTHR11749. 1 hit.
PfamPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFPIRSF001461. RPE. 1 hit.
SUPFAMSSF51366. SSF51366. 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 nameRPEC_CUPNH
AccessionPrimary (citable) accession number: P40117
Secondary accession number(s): Q0K1E4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 13, 2013
This is version 83 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

PATHWAY comments

Index of metabolic and biosynthesis pathways