Hmdb loader
Survey
Identification
HMDB Protein ID HMDBP00204
Secondary Accession Numbers
  • 5436
Name NADPH:adrenodoxin oxidoreductase, mitochondrial
Synonyms
  1. AR
  2. Adrenodoxin reductase
  3. Ferredoxin reductase
  4. Ferredoxin--NADP(+) reductase
Gene Name FDXR
Protein Type Unknown
Biological Properties
General Function Involved in catalytic activity
Specific Function Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.
Pathways
  • cholesterol metabolism
Reactions
reduced adrenodoxin + NADP → oxidized adrenodoxin + NADPH details
Reduced adrenal ferredoxin + NADP + Hydrogen Ion → Oxidized adrenal ferredoxin + NADPH details
GO Classification
Biological Process
cholesterol metabolic process
electron transport chain
steroid biosynthetic process
generation of precursor metabolites and energy
Cellular Component
mitochondrial matrix
mitochondrion
Molecular Function
ferredoxin-NADP+ reductase activity
oxidoreductase activity
nucleotide binding
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 17
Locus 17q24-q25
SNPs FDXR
Gene Sequence
>1476 bp
ATGGCTTCGCGCTGCTGGCGCTGGTGGGGCTGGTCGGCGTGGCCTCGGACCCGGCTGCCT
CCCGCCGGGAGCACCCCGAGCTTCTGCCACCATTTCTCCACACAGGAGAAGACCCCCCAG
ATCTGTGTGGTGGGCAGTGGCCCAGCTGGCTTCTACACGGCCCAACACCTGCTAAAGCAC
CCCCAGGCCCACGTGGACATCTACGAGAAACAGCCTGTGCCCTTTGGCCTGGTGCGCTTT
GGTGTGGCGCCTGATCACCCCGAGGTGAAGAATGTCATCAACACATTTACCCAGACGGCC
CATTCTGGCCGCTGTGCCTTCTGGGGCAACGTGGAGGTGGGCAGGGACGTGACGGTGCCG
GAGCTGCGGGAGGCCTACCACGCTGTGGTGCTGAGCTACGGGGCAGAGGACCATCGGGCC
CTGGAAATTCCTGGTGAGGAGCTGCCAGGTGTGTGCTCCGCCCGGGCCTTCGTGGGCTGG
TACAACGGGCTTCCTGAGAACCAGGAGCTGGAGCCAGACCTGAGCTGTGACACAGCCGTG
ATTCTGGGGCAGGGGAACGTGGCTCTGGACGTGGCCCGCATCCTACTGACCCCACCTGAG
CACCTGGAGAGAACGGACATCACGAAGGCAGCCCTGGGTGTACTGAGGCAGAGTCGAGTG
AAGACAGTGTGGCTAGTGGGCCGGCGTGGACCCCTGCAAGTGGCCTTCACCATTAAGGAG
CTTCGGGAGATGATTCAGTTACCGGGAGCCCGGCCCATTTTGGATCCTGTGGATTTCTTG
GGTCTCCAGGACAAGATCAAGGAGGTCCCCCGCCCGAGGAAGCGGCTGACGGAACTGCTG
CTTCGAACGGCCACAGAGAAGCCAGGGCCGGCGGAAGCTGCCCGCCAGGCATCGGCCTCC
CGTGCCTGGGGCCTCCGCTTTTTCCGAAGCCCCCAGCAGGTGCTGCCCTCACCAGATGGG
CGGCGGGCAGCAGGTGTCCGCCTAGCAGTCACTAGACTGGAGGGTGTCGATGAGGCCACC
CGTGCAGTGCCCACGGGAGACATGGAAGACCTCCCTTGTGGGCTGGTGCTCAGCAGCATT
GGGTATAAGAGCCGCCCTGTCGACCCAAGCGTGCCCTTTGACTCCAAGCTTGGGGTCATC
CCCAATGTGGAGGGCCGGGTTATGGATGTGCCAGGCCTCTACTGCAGCGGCTGGGTGAAG
AGAGGACCTACAGGTGTCATAGCCACAACCATGACTGACAGCTTCCTCACCGGCCAGATG
CTGCTGCAGGACCTGAAGGCTGGGTTGCTCCCCTCTGGCCCCAGGCCTGGCTACGCAGCC
ATCCAGGCCCTGCTCAGCAGCCGAGGGGTCCGGCCAGTCTCTTTCTCAGACTGGGAGAAG
CTGGATGCCGAGGAGGTGGCCCGGGGCCAGGGCACGGGGAAGCCCAGGGAGAAGCTGGTG
GATCCTCAGGAGATGCTGCGCCTCCTGGGCCACTGA
Protein Properties
Number of Residues 491
Molecular Weight 58303.275
Theoretical pI 7.868
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>NADPH:adrenodoxin oxidoreductase, mitochondrial
MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKH
PQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVP
ELREAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAV
ILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKE
LREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASAS
RAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSI
GYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQM
LLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLV
DPQEMLRLLGH
GenBank ID Protein 12804205
UniProtKB/Swiss-Prot ID P22570
UniProtKB/Swiss-Prot Entry Name ADRO_HUMAN
PDB IDs Not Available
GenBank Gene ID BC002960
GeneCard ID FDXR
GenAtlas ID FDXR
HGNC ID HGNC:3642
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Solish SB, Picado-Leonard J, Morel Y, Kuhn RW, Mohandas TK, Hanukoglu I, Miller WL: Human adrenodoxin reductase: two mRNAs encoded by a single gene on chromosome 17cen----q25 are expressed in steroidogenic tissues. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7104-8. [PubMed:2845396 ]
  3. Lin D, Shi YF, Miller WL: Cloning and sequence of the human adrenodoxin reductase gene. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8516-20. [PubMed:2236061 ]