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0SQRD_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionSulfide:quinone oxidoreductase, mitochondrial precursor (ec 1.-.-.-).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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
SequencesProtein: SQRD_HUMAN (450 aa)
mRNA: NM_021199
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00540
  Level 3 annotation:
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 18 residues, 43714547-43714598Exon2: 85 residues, 43738396-43738647Exon3: 59 residues, 43741444-43741615Exon4: 20 residues, 43749417-43749471Exon5: 67 residues, 43753096-43753291Exon6: 72 residues, 43755590-43755800Exon7: 63 residues, 43761967-43762151Exon8: 24 residues, 43767826-43767894Exon9: 61 residues, 43768528-43768707Exon10: 104 residues, 43770462-43770770Exon11: 2 residues, -Jump to SQRD_HUMAN  
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Loci Cluster (Details)Loci: 4169 43561969-43602294 ~-40K 12281(SLC30A4)(-)Loci: 2887 43666708-43689200 ~-22K 12285(PLDN)(+)Loci: 2888 43714547-43770770 ~-56K 12287(SQRDL)(+)Loci: 4168 43196978-43209349 ~-12K 12269(-)Link out to UCSC