Os09g0505700

Functionⁱ

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.

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

Kineticsⁱ

V_max=
16000 µmol/min/mg enzyme
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Identification, cloning, and properties of cytosolic D-ribulose-5-phosphate 3-epimerase from higher plants."
  Kopriva S., Koprivova A., Suess K.-H.
  J. Biol. Chem. 275:1294-1299(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.

Pathwayⁱ: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage).
Proteins known to be involved in this subpathway in this organism are:

Ribulose-phosphate 3-epimerase, cytoplasmic isoform (Os09g0505700)

This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	12	SubstrateBy similarity	1
Metal bindingⁱ	37	Divalent metal cation	1
Active siteⁱ	39	Proton acceptorBy similarity	1
Metal bindingⁱ	39	Divalent metal cation	1
Metal bindingⁱ	70	Divalent metal cation	1
Binding siteⁱ	70	SubstrateBy similarity	1
Active siteⁱ	179	Proton donorBy similarity	1
Metal bindingⁱ	179	Divalent metal cation	1
Binding siteⁱ	181	Substrate; via amide nitrogenBy similarity	1

GO - Molecular functionⁱ

metal ion binding Source: GO_Central
ribulose-phosphate 3-epimerase activity Source: GO_Central

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular carbohydrate metabolic process Source: GO_Central
pentose catabolic process Source: GO_Central
pentose-phosphate shunt, non-oxidative branch Source: GO_Central

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase
Biological process	Carbohydrate metabolism, Pentose shunt
Ligand	Cobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	5.1.3.1 4460
Reactomeⁱ	R-OSA-71336 Pentose phosphate pathway
UniPathwayⁱ	UPA00115;UER00411

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ribulose-phosphate 3-epimerase, cytoplasmic isoform (EC:5.1.3.1) Alternative name(s): Cyt-RPEase Pentose-5-phosphate 3-epimerase Short name: PPE RPEcyt Ribulose-5-phosphate-epimerase
Gene namesⁱ	Ordered Locus Names:Os09g0505700, LOC_Os09g32810
Organismⁱ	Oryza sativa subsp. japonica (Rice)
Taxonomic identifierⁱ	39947 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › Liliopsida › Petrosaviidae › commelinids › Poales › Poaceae › BOP clade › Oryzoideae › Oryzeae › Oryzinae › Oryza › Oryza sativa
Proteomesⁱ	UP000059680 Componentⁱ: Chromosome 9

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000171590	1 – 228	Ribulose-phosphate 3-epimerase, cytoplasmic isoformAdd BLAST		228

Proteomic databases

PaxDbⁱ	Q9SE42

PaxDbⁱ

Q9SE42

Expressionⁱ

Tissue specificityⁱ

Predominantly accumulates in roots and seedlings.1 Publication

Gene expression databases

ExpressionAtlasⁱ	Q9SE42 differential
Genevisibleⁱ	Q9SE42 OS

Interactionⁱ

Subunit structureⁱ

Homodimer.2 Publications

Protein-protein interaction databases

STRINGⁱ	39947.LOC_Os09g32810.1

STRINGⁱ

39947.LOC_Os09g32810.1

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	8 – 12	Combined sources	5
Helixⁱ	13 – 15	Combined sources	3
Helixⁱ	18 – 20	Combined sources	3
Helixⁱ	21 – 30	Combined sources	10
Beta strandⁱ	34 – 47	Combined sources	14
Helixⁱ	53 – 60	Combined sources	8
Beta strandⁱ	65 – 74	Combined sources	10
Helixⁱ	76 – 79	Combined sources	4
Helixⁱ	80 – 86	Combined sources	7
Beta strandⁱ	89 – 94	Combined sources	6
Helixⁱ	95 – 97	Combined sources	3
Turnⁱ	99 – 101	Combined sources	3
Helixⁱ	102 – 111	Combined sources	10
Beta strandⁱ	115 – 120	Combined sources	6
Helixⁱ	126 – 129	Combined sources	4
Helixⁱ	130 – 134	Combined sources	5
Beta strandⁱ	135 – 137	Combined sources	3
Beta strandⁱ	140 – 147	Combined sources	8
Beta strandⁱ	149 – 151	Combined sources	3
Helixⁱ	158 – 160	Combined sources	3
Helixⁱ	161 – 170	Combined sources	10
Beta strandⁱ	174 – 181	Combined sources	8
Turnⁱ	184 – 186	Combined sources	3
Helixⁱ	187 – 193	Combined sources	7
Beta strandⁱ	197 – 201	Combined sources	5
Helixⁱ	202 – 205	Combined sources	4
Helixⁱ	210 – 223	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9SE42
SMRⁱ	Q9SE42
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9SE42

EvolutionaryTraceⁱ

Q9SE42

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	150 – 153	Substrate bindingBy similarity		4
Regionⁱ	201 – 202	Substrate bindingBy similarity		2

Sequence similaritiesⁱ

Belongs to the ribulose-phosphate 3-epimerase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3111 Eukaryota COG0036 LUCA
HOGENOMⁱ	HOG000259349
InParanoidⁱ	Q9SE42
KEGG Orthology (KO) More...KOⁱ	K01783
OMAⁱ	ISVHYES
Database of Orthologous Groups More...OrthoDBⁱ	EOG09360LI4

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00429 RPE, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR026019 Ribul_P_3_epim IPR000056 Ribul_P_3_epim-like IPR011060 RibuloseP-bd_barrel
PANTHERⁱ	PTHR11749 PTHR11749, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00834 Ribul_P_3_epim, 1 hit
PIRSFⁱ	PIRSF001461 RPE, 1 hit
SUPFAMⁱ	SSF51366 SSF51366, 1 hit
TIGRFAMsⁱ	TIGR01163 rpe, 1 hit
PROSITEⁱ	View protein in PROSITE PS01085 RIBUL_P_3_EPIMER_1, 1 hit PS01086 RIBUL_P_3_EPIMER_2, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.ⁱShow all

Q9SE42-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAAAAAAKIA PSMLSSDFAN LAAEADRMVR LGADWLHMDI MDGHFVPNLT 
        60         70         80         90        100
IGAPVIQSLR KHTKAYLDCH LMVTNPSDYV EPLAKAGASG FTFHIEVSRD 
       110        120        130        140        150
NWQELIQSIK AKGMRPGVSL RPGTPVEEVF PLVEAENPVE LVLVMTVEPG 
       160        170        180        190        200
FGGQKFMPEM MEKVRALRKK YPSLDIEVDG GLGPSTIDVA ASAGANCIVA 
       210        220 
GSSIFGAAEP GEVISALRKS VEGSQNKS

Length:228

Mass (Da):24,291

Last modified:May 1, 2000 - v1

Checksum:ⁱED2FD8F9F230226B

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation
	A0A0P0XQA9	A0A0P0XQA9_ORYSJ		Os09g0505700 protein Os09g0505700 protein	Os09g0505700 OSNPB_090505700	205	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	42 – 43	DG → GR (PubMed:16100779).Curated		2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF189365 mRNA Translation: AAF01048.1 AC108753 Genomic DNA No translation available. AP008215 Genomic DNA Translation: BAF25518.2 AP014965 Genomic DNA Translation: BAT08853.1 AK069451 mRNA Translation: BAG91440.1
NCBI Reference Sequences More...RefSeqⁱ	XP_015611665.1, XM_015756179.1
UniGeneⁱ	Os.8665

Genome annotation databases

EnsemblPlantsⁱ	Os09t0505700-02; Os09t0505700-02; Os09g0505700
GeneIDⁱ	4347508
Grameneⁱ	Os09t0505700-02; Os09t0505700-02; Os09g0505700
KEGGⁱ	osa:4347508

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9SE42	Ribulose-phosphate 3-epimerase		ORYRU		228	UniRef100_Q9SE42
Ribulose-phosphate 3-epimerase		ORYNI		228
Ribulose-phosphate 3-epimerase		ORYSI		228

Protein	Similar proteins		Species	Score	Length	Source
Q9SE42	Ribulose-phosphate 3-epimerase		ORYRU		228	UniRef90_Q9SE42
Ribulose-phosphate 3-epimerase		ORYNI		228
Ribulose-phosphate 3-epimerase		ORYSI		228
Ribulose-phosphate 3-epimerase		Oryza glumipatula		228
Ribulose-phosphate 3-epimerase		Panicum hallii		228
+15

Protein	Similar proteins		Species	Score	Length	Source
Q9SE42	Ribulose-phosphate 3-epimerase		ORYRU		228	UniRef50_Q9SE42
Ribulose-phosphate 3-epimerase		ORYNI		228
Ribulose-phosphate 3-epimerase		ORYSI		228
Ribulose-phosphate 3-epimerase		Oryza glumipatula		228
Ribulose-phosphate 3-epimerase		Panicum hallii		228
+152

Entry informationⁱ

Entry nameⁱ	RPE1_ORYSJ
Accessionⁱ	Q9SE42Primary (citable) accession number: Q9SE42 Secondary accession number(s): B7EGE3, Q0J0L5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
	Last sequence update:	May 1, 2000
	Last modified:	September 12, 2018
	This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Plant Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9SE42 (RPE1_ORYSJ)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Ribulose-phosphate 3-epimerase, cytoplasmic isoform

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: pentose phosphate pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Cytosol

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi