Reviewed, UniProtKB/Swiss-Prot Q43157 (RPE_SPIOL)

Names and origin

Protein names

Recommended name:
    Ribulose-phosphate 3-epimerase, chloroplastic
    EC=5.1.3.1
Alternative name(s):
    Pentose-5-phosphate 3-epimerase
      Short name=PPE
    R5P3E
      Short name=RPE

Gene names

Name:

RPE

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-ribulose 5-phosphate = D-xylulose 5-phosphate. Ref.1 Ref.2
Pathway	Carbohydrate biosynthesis; Calvin cycle.
Subunit structure	Homooctamer. Ref.2
Subcellular location	Plastid › chloroplast thylakoid membrane. Ref.3
Sequence similarities	Belongs to the ribulose-phosphate 3-epimerase family.
Biophysicochemical properties	Kinetic parameters: KM=250 µM for ribulose 5-phosphate pH dependence: Optimum pH is 8.5.

Ontologies

Keywords
Biological process	Calvin cycle Carbohydrate metabolism Pentose shunt
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide
Molecular function	Isomerase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Ref.1 Non-traceable author statement. Source: UniProtKB reductive pentose-phosphate cycle Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	chloroplast thylakoid membrane Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	ribulose-phosphate 3-epimerase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 50	50	Chloroplast Ref.3
	Chain	51 – 285	235	Ribulose-phosphate 3-epimerase, chloroplastic		PRO_0000025416
Sites
	Active site	236	1	Electrophile Probable
Experimental info
	Mutagenesis	236	1	D → A, E or N: Change in activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q43157-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: ED0236FB7B629512	FASTA	285	30,366
	10 20 30 40 50 60 MSAASLCQST LQSQINGFCG GLNIRKLQPS TSSPNSLTFT RRKVQTLVKA TSRVDKFSKS 70 80 90 100 110 120 DIIVSPSILS ANFAKLGEQV KAVELAGCDW IHVDVMDGRF VPNITIGPLV VDALRPVTDL 130 140 150 160 170 180 PLDVHLMIVE PEQRVPDFIK AGADIVSVHC ELASTIHLHR TVNQIKSLGA KAGVVLNPGT 190 200 210 220 230 240 PLSTIEYVLD VVDLVLIMSV NPGFGGQSFI ESQVKKISDL RKMCVEKGVN PWIEVDGGVT 250 260 270 280 PANAYKVIEA GANALVAGSA VFGAKDYAEA IKGIKASKRP EPVAV

References

[1]	"Cloning of the amphibolic Calvin cycle/OPPP enzyme D-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and evolutionary aspects." Nowitzki U., Wyrich R., Westhoff P., Henze K., Schnarrenberger C., Martin W.F. Plant Mol. Biol. 29:1279-1291(1995) [PubMed: 8616224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[2]	"D-ribulose-5-phosphate 3-epimerase: cloning and heterologous expression of the spinach gene, and purification and characterization of the recombinant enzyme." Chen Y.-R., Hartman F.C., Lu T.-Y.S., Larimer F.W. Plant Physiol. 118:199-207(1998) [PubMed: 9733539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT. Strain: cv. Melody.
[3]	"Purification, properties and in situ localization of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts." Teige M., Melzer M., Suess K.-H. Eur. J. Biochem. 252:237-244(1998) [PubMed: 9523694] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-66, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Strain: cv. Matador.
[4]	"Identification of a catalytic aspartyl residue of D-ribulose 5-phosphate 3-epimerase by site-directed mutagenesis." Chen Y.-R., Larimer F.W., Serpersu E.H., Hartman F.C. J. Biol. Chem. 274:2132-2136(1999) [PubMed: 9890975] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS OF ASP-236.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42328 mRNA. Translation: AAC41677.1. AF070941 mRNA. Translation: AAC24708.1.
PIR	S62724.
3D structure databases
HSSP	HSSP built from PDB template 1RPX based on UniProtKB Q43843.
SMR	Q43157. Positions 52-281.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.1.3.1. 286.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR000056. Ribul_P_3_epim. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11749. Ribul_P_3_epim. 1 hit.
Pfam	PF00834. Ribul_P_3_epim. 1 hit. [Graphical view]
TIGRFAMs	TIGR01163. rpe. 1 hit.
PROSITE	PS01085. RIBUL_P_3_EPIMER_1. 1 hit. PS01086. RIBUL_P_3_EPIMER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPE_SPIOL

Accession

Primary (citable) accession number: Q43157

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 5, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)