Reviewed, UniProtKB/Swiss-Prot Q43843 (RPE_SOLTU)

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
Organism	Solanum tuberosum (Potato)
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	280 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts xylulose 5-phosphate to ribulose 5-phosphate via epimerization.
Catalytic activity	D-ribulose 5-phosphate = D-xylulose 5-phosphate.
Pathway	Carbohydrate biosynthesis; Calvin cycle.
Subunit structure	Homohexamer.
Subcellular location	Plastid › chloroplast thylakoid membrane.
Tissue specificity	Highest level of expression in leaves, whereas it is low in roots, tubers, and stems.
Sequence similarities	Belongs to the ribulose-phosphate 3-epimerase family.

Ontologies

Keywords
Biological process	Calvin cycle Carbohydrate metabolism Pentose shunt
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide
Molecular function	Isomerase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast thylakoid membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ribulose-phosphate 3-epimerase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

‹1 – 45

›45

Chloroplast

Chain

46 – 280

235

Ribulose-phosphate 3-epimerase, chloroplastic

PRO_0000025417

Experimental info

Non-terminal residue

1

1

Secondary structure

1

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280

Helix Strand Turn

Details...

Helix

48 – 51

4

Beta strand

58 – 62

5

Helix

63 – 65

3

Helix

68 – 70

3

Helix

71 – 80

10

Beta strand

86 – 97

12

Helix

103 – 109

7

Helix

110 – 112

3

Beta strand

117 – 125

9

Helix

126 – 135

10

Beta strand

139 – 144

6

Turn

147 – 149

3

Helix

153 – 162

10

Beta strand

165 – 171

7

Helix

177 – 180

4

Turn

181 – 186

6

Beta strand

188 – 195

8

Helix

208 – 222

15

Beta strand

227 – 233

7

Turn

236 – 238

3

Helix

239 – 245

7

Beta strand

249 – 253

5

Helix

254 – 257

4

Helix

262 – 270

9

Sequences

	Sequence		Length	Mass (Da)
	Q43843-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 3381A798F056491C	FASTA	280	29,881
	10 20 30 40 50 60 SLGSSTLLQS QISGFGGSQK LQKISFSNPN SLTFTRRRIQ TVVNASSRVD KFSKSDIIVS 70 80 90 100 110 120 PSILSANFSK LGEQVKAIEQ AGCDWIHVDV MDGRFVPNIT IGPLVVDSLR PITDLPLDVH 130 140 150 160 170 180 LMIVEPDQRV PDFIKAGADI VSVHCEQSST IHLHRTINQI KSLGAKAGVV LNPGTPLTAI 190 200 210 220 230 240 EYVLDAVDLV LIMSVNPGFG GQSFIESQVK KISDLRKICA ERGLNPWIEV DGGVGPKNAY 250 260 270 280 KVIEAGANAL VAGSAVFGAP DYAEAIKGIK TSKRPEAVAV

References

[1]	"Chloroplast pentose-5-phosphate 3-epimerase from potato: cloning, cDNA sequence, and tissue-specific enzyme accumulation." Teige M., Kopriva S., Bauwe H., Suess K.-H. FEBS Lett. 377:349-352(1995) [PubMed: 8549753] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Desiree. Tissue: Leaf.
[2]	"Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts." Kopp J., Kopriva S., Suess K.-H., Schulz G.E. J. Mol. Biol. 287:761-771(1999) [PubMed: 10191144] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z50098 mRNA. Translation: CAA90426.1.

PIR

S68407.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RPX	X-ray	2.30	A/B/C	47-276	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

5.1.3.1. 296.

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_SOLTU

Accession

Primary (citable) accession number: Q43843

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 20, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)