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0PCYOX_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePCYOX1
DescriptionPrenylcysteine oxidase precursor (ec 1.8.3.5) (pcl1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005764 lysosome (NAS)
0016829 lyase activity (NAS)
0030327 prenylated protein catabolism (NAS)
0030329 prenylcysteine metabolism (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This family contains prenylcysteine lyases () that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines.roducing free cysteine.n isoprenoid aldehyde and hydrogen peroxide as products of the reaction . It has been noted that this enzyme has considerable homology with ClP55. 55 kDa protein that is associated with chloride ion pumps .
  IPR010795:Prenylcysteine lyase
This entry describes both class I and class II oxidoreductases. FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase.rypanothione reductase.ipoamide dehydrogenase.ercuric reductase.hioredoxin reductase.lkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases.n particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase.utidaredoxin reductase.erpredoxin reductase.erredoxin-NAD+ reductase components of benzene 1.-dioxygenase.oluene 1.-dioxygenase.hlorobenzene dioxygenase.iphenyl dioxygenase).ADH oxidase and NADH peroxidase . Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites.uggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently . Despite functional similarities.xidoreductases of this family show no sequence similarity with adrenodoxin reductases and flavoprotein pyridine nucleotidecytochrome reductases (FPNCR) . Assuming that disulphide reductase activity emerged later.uring divergent evolution.he family can be referred to as FAD-dependent pyridine nucleotide reductases.ADPNR.To date.D structures of glutathione reductase .hioredoxin reductase .ercuric reductase .ipoamide dehydrogenase .rypanothione reductase and NADH peroxidase have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta fold.ut the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly. By contrast with the FPNCR family.he folds of the FAD- and NAD(P)H-binding domains are similar.uggesting that the domains evolved by gene duplication .
  IPR013027:FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR010795:Prenylcys_lyase 
Evalue:-283.259643554687 
Location:128-505IPR013027:Pyr_redox_2 
Evalue:-8.6777811050415 
Location:36-73
SequencesProtein: PCYOX_HUMAN (505 aa)
mRNA: BC022259 NM_016297
Local Annotation
Synapse Ontology
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentK05906
  Level 3 annotation:
    prenylcysteine oxidase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 43 residues, 70338784-70338912Exon2: 71 residues, 70339995-70340202Exon3: 60 residues, 70341847-70342022Exon4: 72 residues, 70355594-70355806Exon5: 53 residues, 70356149-70356302Exon6: 268 residues, 70357369-70358167Exon7: 2 residues, -Jump to PCYOX_HUMANExon1: 39 residues, 70338796-70338912Exon2: 71 residues, 70339995-70340202Exon3: 60 residues, 70341847-70342022Exon4: 72 residues, 70355594-70355806Exon5: 53 residues, 70356149-70356302Exon6: 1118 residues, 70357369-70360718Exon7: 2 residues, -Jump to PCYOX_HUMAN  
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