P56188 (RPE_HELPY) 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:	HP_1386

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	217 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	pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro
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 – 217	217	Ribulose-phosphate 3-epimerase		PRO_0000171572
Regions
	Region	138 – 141	4	Substrate binding By similarity
	Region	193 – 194	2	Substrate binding By similarity
Sites
	Active site	31	1	Proton acceptor By similarity
	Active site	171	1	Proton donor By similarity
	Metal binding	29	1	Divalent metal cation By similarity
	Metal binding	31	1	Divalent metal cation By similarity
	Metal binding	62	1	Divalent metal cation By similarity
	Metal binding	171	1	Divalent metal cation By similarity
	Binding site	6	1	Substrate By similarity
	Binding site	62	1	Substrate By similarity
	Binding site	173	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56188 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 7CAA9E1E5DC9006F	FASTA	217	24,045
	10 20 30 40 50 60 MKVAPSLLSA DFMHLAKEIE SVSNADFLHV DVMDGHYVPN LTMGPVVLEN VTQMSQVPLD 70 80 90 100 110 120 VHLMVENASF FAELFAPLKP QIISIHAENE KHPHRVLQLI KNLGITPGIV LNPHTHEESI 130 140 150 160 170 180 KYLLESVGLV LLMSVNPGFG GQKFLDLVLE KCLKVKELIK RYNPSCLLEV DGGVNDKNIF 190 200 210 ELQQAGVDVV VSGSYIFKSK DRKLAIEGLQ NVRQSLA

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD08425.1.
PIR	B64693.
RefSeq	NP_208177.1. NC_000915.1. YP_006935309.1. NC_018939.1.
3D structure databases
ProteinModelPortal	P56188.
ModBase	Search...
Protein-protein interaction databases
STRING	85962.HP1386.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD08425; AAD08425; HP_1386.
GeneID	13870596. 900293.
KEGG	heo:C694_07155. hpy:HP1386.
PATRIC	20594161. VBIHelPyl33062_1451.
Phylogenomic databases
eggNOG	COG0036.
KO	K01783.
OMA	LFAPLNP.
ProtClustDB	PRK05581.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR026019. Ribul_P_3_epim. IPR000056. Ribul_P_3_epim-like. IPR011060. RibuloseP-bd_barrel. [Graphical view]
PANTHER	PTHR11749. PTHR11749. 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_HELPY

Accession

Primary (citable) accession number: P56188

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program