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InterPro: IPR010795 Prenylcysteine lyase

Protein matches Help

UniProtKB

Matches:

85 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR010795 Prenylcys_lyase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07156	Prenylcys_lyase	85
Signatures in BioMart

InterPro Relationships Help

Found in

IPR017046 Prenylcysteine oxidase

GO Term annotation Help

Process

GO:0030328 prenylcysteine catabolic process
GO:0055114 oxidation reduction

Function

GO:0016670 oxidoreductase activity, acting on sulfur group of donors, oxygen as acceptor

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a conserved region found in a group of prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction [1]. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps [2].

Database links Help

Enzyme: EC:1.8.3

PANDIT: PF07156

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010795

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P57681 Probable prenylcysteine oxidase

Q0P5H1 Prenylcysteine oxidase-like

Q8C7K6 Prenylcysteine oxidase-like

Q8NBM8 Prenylcysteine oxidase-like

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006076	FAD dependent oxidoreductase
IPR010795	Prenylcysteine lyase
IPR017046	Prenylcysteine oxidase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Digits JA, Pyun HJ, Coates RM, Casey PJ. Stereospecificity and kinetic mechanism of human prenylcysteine lyase, an unusual thioether oxidase. J. Biol. Chem. 277 41086-93 2002 [PubMed: 12186880] http://dx.doi.org/10.1074/jbc.M208069200
2.	Kitagawa K, Yagyu K, Yamamoto A, Hattori N, Omori K, Zeng XT, Inagaki C. Molecular cloning and characterization of the Cl(-) pump-associated 55-kDa protein in rat brain. Biochem. Biophys. Res. Commun. 289 363-71 2001 [PubMed: 11716481] http://dx.doi.org/10.1006/bbrc.2001.5997

InterPro 23.1