Q58093 (RPE_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribulose-phosphate 3-epimerase
EC=5.1.3.1

Alternative name(s):
Pentose-5-phosphate 3-epimerase
Short name=PPE
R5P3E

Gene names

Name:	rpe
Ordered Locus Names:	MJ0680

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Protein existence	Inferred 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+, Mn2+ and Zn2+ By similarity.
Sequence similarities	Belongs to the ribulose-phosphate 3-epimerase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Cobalt Manganese Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribulose-phosphate 3-epimerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 234	234	Ribulose-phosphate 3-epimerase		PRO_0000171584
Regions
	Region	139 – 142	4	Substrate binding By similarity
	Region	194 – 195	2	Substrate binding By similarity
Sites
	Active site	34	1	Proton acceptor By similarity
	Active site	172	1	Proton donor By similarity
	Metal binding	32	1	Divalent metal cation By similarity
	Metal binding	34	1	Divalent metal cation By similarity
	Metal binding	65	1	Divalent metal cation By similarity
	Metal binding	172	1	Divalent metal cation By similarity
	Binding site	7	1	Substrate By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	174	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58093 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 070E2CF7A2BC9D7F	FASTA	234	25,838
	10 20 30 40 50 60 MIKIGASILS ADFGHLREEI KKAEEAGVDF FHVDMMDGHF VPNISMGIGI AKHVKKLTEL 70 80 90 100 110 120 PVEVHLMVEN VDLFVNEFEE MDYITFHIEA VKFPFRIINR IKSIGAKPIV ALNPATPLDA 130 140 150 160 170 180 IEYILGDVYA VLVMTVEPGF SGQKFIPVMT KKIRKLKSMI VENGYDTKIF VDGGINVETA 190 200 210 220 230 PLAVKAGADV LVAASAIFGK DDVKTAVKNL REAALEALNK DFLTKSFNSN EEKQ

References

[1]

"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB98675.1.
PIR	H64384.
RefSeq	NP_247664.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58093.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1451546.
GenomeReviews	Gene locus MJ0680 in contig L77117_GR.
KEGG	mja:MJ_0680.
NMPDR	fig|243232.1.peg.701.
TIGR	MJ0680.
Phylogenomic databases
HOGENOM	HBG571751.
OMA	VMDRLDM.
ProtClustDB	CLSK876291.
Enzyme and pathway databases
BioCyc	MJAN243232:MJ_0680-MONOMER.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR000056. Ribul_P_3_epim. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01783.
PANTHER	PTHR11749. Ribul_P_3_epim. 1 hit.
Pfam	PF00834. Ribul_P_3_epim. 1 hit. [Graphical view]
PIRSF	PIRSF001461. RPE. 1 hit.
SUPFAM	SSF51366. RibP_bind_barrel. 1 hit.
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_METJA

Accession

Primary (citable) accession number: Q58093

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program