SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0ADRO_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFDXR
DescriptionNadph:adrenodoxin oxidoreductase, mitochondrial precursor (ec 1.18.1.2) (adrenodoxin reductase) (ar) (ferredoxin--nadp(+) reductase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0004324 ferredoxin-NADP+ reductase activity (TAS)
0006118 electron transport (TAS)
0006694 steroid biosynthesis (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/51856139.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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 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
Mitochondrial P450-containing systems comprise 3 components.n FAD-containing flavoprotein NADPH:adrenodoxin reductase (AR); an iron-sulphur protein.drenodoxin; and P450 . The direction of electron flow is NADPH to AR to adrenodoxin to P450. FAD can be reduced by 2 electrons from NADPH.hich are transferred one at a time to adrenodoxin. one-electron carrier. Both AR and adrenodoxin are soluble proteins located on the matrix side of the inner mitochondrial membrane. Despite functional parallels.R shows no global similarity either to flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) or to FAD-dependent pyridine nucleotide reductases (FADPNR) . However.LAST searches reveal local similarity of the N-terminal region of AR to glutamate synthase and NADH peroxidase.specially in the nucleotide-binding regions.uggesting that AR and FADPNR may be distantly related.
  IPR000759:Adrenodoxin reductase
IPR013027:Pyr_redox_2 
Evalue:-3.619788646698 
Location:40-70IPR000759:ADXRDTASE 
Evalue:0 
Location:179-193IPR000759:ADXRDTASE 
Evalue:0 
Location:246-259IPR000759:ADXRDTASE 
Evalue:0 
Location:107-117
SequencesProtein: ADRO_HUMAN (491 aa)
mRNA: CR594512 NM_004110 NM_024417
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 assignmentK00528
  Level 3 annotation:
    ferredoxin--NADP+ reductase
  Level 2 annotation:
    Other energy metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 149 residues, 70370220-70370664Exon2: 59 residues, 70370792-70370963Exon3: 59 residues, 70371612-70371784Exon4: 68 residues, 70371864-70372064Exon5: 30 residues, 70372196-70372281Exon6: 44 residues, 70372540-70372666Exon7: 36 residues, 70373435-70373537Exon8: 40 residues, 70373847-70373961Exon9: 43 residues, 70374162-70374285Exon10: 33 residues, 70374500-70374593Exon11: 34 residues, 70379755-70379853Exon12: 37 residues, 70380585-70380692Exon13: 2 residues, -Jump to ADRO_HUMANExon1: 148 residues, 70370221-70370664Exon2: 59 residues, 70370792-70370963Exon3: 59 residues, 70371612-70371784Exon4: 68 residues, 70371864-70372064Exon5: 30 residues, 70372196-70372281Exon6: 38 residues, 70372540-70372648Exon7: 36 residues, 70373435-70373537Exon8: 40 residues, 70373847-70373961Exon9: 43 residues, 70374162-70374285Exon10: 33 residues, 70374500-70374593Exon11: 34 residues, 70379755-70379853Exon12: 37 residues, 70380585-70380692Exon13: 2 residues, -Jump to ADRO_HUMANExon1: 140 residues, 70370245-70370664Exon2: 59 residues, 70370792-70370963Exon3: 59 residues, 70371612-70371784Exon4: 68 residues, 70371864-70372064Exon5: 30 residues, 70372196-70372281Exon6: 38 residues, 70372540-70372648Exon7: 36 residues, 70373435-70373537Exon8: 40 residues, 70373847-70373961Exon9: 43 residues, 70374162-70374285Exon10: 34 residues, 70374500-70374596Exon11: 34 residues, 70379755-70379853Exon12: 43 residues, 70380585-70380710Exon13: 2 residues, -Jump to ADRO_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3038 70178864-70255068 ~-76K 16552(+)Loci: 3039 70256378-70277089 ~-21K 16559(SLC9A3R1)(+)Loci: 4310 70349762-70367602 ~-18K 16565(GRIN2C)(-)Loci: 4311 70370220-70380710 ~-10K 16567(FDXR)(-)Loci: 4312 70546549-70554669 ~-8K 16577(ATP5H)(-)Loci: 4313 70637918-70639472 ~-2K 16582(NT5C)(-)Loci: 4314 70744289-70769272 ~-25K 16589(GGA3)(-)Loci: 4315 70780668-70797109 ~-16K 16594(SLC25A19)(-)Loci: 4316 71265612-71272875 ~-7K 16620(GALK1)(-)Loci: 4317 71514521-71534972 ~-20K 16639(EVPL)(-)Loci: 4318 71546785-71580202 ~-33K 16642(SRP68)(-)Loci: 3040 71582486-71585168 ~-3K 16644(GALR2)(+)Loci: 3041 71586857-71590480 ~-4K 16645(+)Loci: 4319 71588681-71611451 ~-23K 16647(EXOC7)(-)Loci: 3037 69833964-69859062 ~-25K 16537(+)Link out to UCSC