Protein Annotations for Ribulose-5-phosphate-epimerase, RPE1

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Name	Gene Symbol	Rec Full Name	Protein Information	Quick Quote	Price, Turnaround
RPE1_ORYSJ, Oryza sativa Japonica Group ()		Ribulose-5-phosphate-epimerase	Functions		Starting from $1600, 4 weeks
RPE1_ORYSJ, Oryza sativa Japonica Group ()		Ribulose-5-phosphate-epimerase	Protein Domains		Quote

Protein Names

Recommended name:	Ribulose-phosphate 3-epimerase, cytoplasmic isoform;
Alternative name(s):	Cyt-RPEase Pentose-5-phosphate 3-epimerase RPEcyt Ribulose-5-phosphate-epimerase

Protein IDs
(Accession numbers)

UniProtKB	Q9SE42
NCBI RefSeq	NP_001063604.2, NM_001070139.2.

Organism

Latin Name/ (Common Name)	Oryza sativa subsp. japonica (Rice).
Taxonomic Identifier (NCBI)	39947

Gene Names

[GenPool]

GeneID

4347508

Genome
Annotation (Ensembl)

Protein Sequence

SEQUENCE   228 AA;  24291 MW;  ED2FD8F9F230226B CRC64;
MAAAAAAKIA PSMLSSDFAN LAAEADRMVR LGADWLHMDI MDGHFVPNLT IGAPVIQSLR
KHTKAYLDCH LMVTNPSDYV EPLAKAGASG FTFHIEVSRD NWQELIQSIK AKGMRPGVSL
RPGTPVEEVF PLVEAENPVE LVLVMTVEPG FGGQKFMPEM MEKVRALRKK YPSLDIEVDG
GLGPSTIDVA ASAGANCIVA GSSIFGAAEP GEVISALRKS VEGSQNKS

General annotation

Function	Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate.
Cofactor	Binds 1 divalent metal cation per subunit. Active with Co(2+), Mn(2+) and Zn(2+) (By similarity).
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Predominantly accumulates in roots and seedlings.
Induction
Domain
Post-translational modification
Involvement in disease

References

"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)., PubMeb:10625676 DOI:10.1074/jbc.275.2.1294
"The map-based sequence of the rice genome.";,Nature 436:793-800(2005).,PubMeb:16100779 DOI:10.1038/nature03895
"Structure and catalytic mechanism of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice.";,Jelakovic S., Kopriva S., Suess K.-H., Schulz G.E.;,J. Mol. Biol. 326:127-135(2003).,PubMeb:12547196 DOI:10.1016/S0022-2836(02)01374-8

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Protein Domain Databases

InterPro	IPR013785, Aldolase_TIM. IPR000056, Ribul_P_3_epim. IPR011060, RibuloseP-bd_barrel.
Gene3D	G3DSA:3.20.20.70, Aldolase_TIM; 1.
PANTHER	PTHR11749, Ribul_P_3_epim; 1.
Pfam	PF00834, Ribul_P_3_epim; 1.
PRINTS
SUPFAM	SSF51366, RibP_bind_barrel; 1.
PROSITE	PS01085, RIBUL_P_3_EPIMER_1; 1. PS01086, RIBUL_P_3_EPIMER_2; 1.

3D Structure
Database (PDB)

Entry	Method	Resolution (A)	Chain	Positions	PDBsum
1H1Y	X-ray	1.87 A	A/B	1-228	[>>]
1H1Z	X-ray	3.40 A	A/B	1-228	[>>]

Sequence
Annotation

Feature key	Position(s)	Length	Description
Polypeptide chain	1 - 228	228	Ribulose-phosphate 3-epimerase, /FTId=PRO_0000171590.
Region	150 - 153	4	Substrate binding (By similarity).
Region	201 - 202	2	Substrate binding (By similarity).
Amino acid(s)	39	1	Proton acceptor (By similarity).
Amino acid(s)	179	1	Proton donor (By similarity).
Metal ion	37	1	Divalent metal cation.
Metal ion	39	1	Divalent metal cation.
Metal ion	70	1	Divalent metal cation.
Metal ion	179	1	Divalent metal cation.
Binding	12	1	Substrate (By similarity).
Binding	70	1	Substrate (By similarity).
Binding	181	1	Substrate; via amide nitrogen (By
Different sources report differing sequences	42 - 43	2	DG -> GR (in Ref. 2).
Strand	8 - 12	5
Strand	34 - 47	14
Strand	65 - 74	10
Strand	89 - 94	6
Strand	115 - 120	6
Strand	135 - 137	3
Strand	140 - 147	8
Strand	174 - 181	8
Strand	197 - 201	5
Helix	13 - 15	3
Helix	18 - 20	3
Helix	21 - 30	10
Helix	53 - 60	8
Helix	76 - 79	4
Helix	80 - 86	7
Helix	95 - 97	3
Helix	102 - 111	10
Helix	126 - 129	4
Helix	130 - 134	5
Helix	158 - 160	3
Helix	161 - 170	10
Helix	187 - 193	7
Helix	202 - 205	4
Helix	210 - 223	14
Turn	99 - 101	3
Turn	184 - 186	3

Protein-protein
Interaction
Databases

DIP
IntAct
MINT
STRING	Q9SE42

Binary Interactions

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Entry

#Exp.

IntAct

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Database (CTD)

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