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NameAdrenodoxin, mitochondrial
Synonyms
  • Adrenal ferredoxin
  • ADX
  • Ferredoxin-1
  • Hepatoredoxin
Gene NameFDX1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010215|Adrenodoxin, mitochondrial
MAAAGGARLLRAASAVLGGPAGRWLHHAGSRAGSSGLLRNRGPGGSAEASRSLSVSARAR
SSSEDKITVHFINRDGETLTTKGKVGDSLLDVVVENNLDIDGFGACEGTLACSTCHLIFE
DHIYEKLDAITDEENDMLDLAYGLTDRSRLGCQICLTKSMDNMTVRVPETVADARQSIDV
GKTS
Number of residues184
Molecular Weight19392.475
Theoretical pI5.62
GO Classification
Functions
  • iron ion binding
  • electron carrier activity
  • 2 iron, 2 sulfur cluster binding
Processes
  • C21-steroid hormone biosynthetic process
  • hormone biosynthetic process
  • sterol metabolic process
  • small molecule metabolic process
  • oxidation-reduction process
  • steroid metabolic process
  • cholesterol metabolic process
  • xenobiotic metabolic process
Components
  • mitochondrion
  • mitochondrial matrix
General FunctionIron ion binding
Specific FunctionParticipates in the synthesis of thyroid hormones. Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID557734
UniProtKB IDP10109
UniProtKB Entry NameADX_HUMAN
Cellular LocationMitochondrion matrix
Gene sequence
>lcl|BSEQ0010216|Adrenodoxin, mitochondrial (FDX1)
ATGGCTGCCGCTGGGGGCGCCCGGCTGCTGCGCGCCGCTTCTGCTGTCCTCGGCGGCCCG
GCCGGCCGGTGGCTGCACCACGCTGGGTCCCGCGCTGGATCCAGCGGCCTGCTGAGGAAC
CGGGGGCCGGGCGGGAGCGCGGAGGCGAGCCGGTCGCTGAGCGTGTCGGCGCGGGCCCGG
AGCAGCTCAGAAGATAAAATAACAGTCCACTTTATAAACCGTGATGGTGAAACATTAACA
ACCAAAGGAAAAGTTGGTGATTCTCTGCTAGATGTTGTGGTTGAAAATAATCTAGATATT
GATGGCTTTGGTGCATGTGAGGGAACCCTGGCTTGTTCAACCTGTCACCTCATCTTTGAA
GATCACATATATGAGAAGTTAGATGCAATCACTGATGAGGAGAATGACATGCTCGATCTG
GCATATGGACTAACAGACAGATCACGGTTGGGCTGCCAAATCTGTTTGACAAAATCTATG
GACAATATGACTGTTCGAGTGCCTGAAACAGTGGCTGATGCCAGACAATCCATTGATGTG
GGCAAGACCTCCTGA
GenBank Gene IDM23668
GeneCard IDNot Available
GenAtlas IDFDX1
HGNC IDHGNC:3638
Chromosome Location11
Locus11q22
References
  1. Chang CY, Wu DA, Lai CC, Miller WL, Chung BC: Cloning and structure of the human adrenodoxin gene. DNA. 1988 Nov;7(9):609-15. 3229285
  2. Picado-Leonard J, Voutilainen R, Kao LC, Chung BC, Strauss JF 3rd, Miller WL: Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. J Biol Chem. 1988 Mar 5;263(7):3240-4. 3343244
  3. Mittal S, Zhu YZ, Vickery LE: Molecular cloning and sequence analysis of human placental ferredoxin. Arch Biochem Biophys. 1988 Aug 1;264(2):383-91. 2969697
  4. Chang CY, Wu DA, Mohandas TK, Chung BC: Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family. DNA Cell Biol. 1990 Apr;9(3):205-12. 2340092
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  8. Sheftel AD, Stehling O, Pierik AJ, Elsasser HP, Muhlenhoff U, Webert H, Hobler A, Hannemann F, Bernhardt R, Lill R: Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis. Proc Natl Acad Sci U S A. 2010 Jun 29;107(26):11775-80. doi: 10.1073/pnas.1004250107. Epub 2010 Jun 14. 20547883
  9. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  10. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  11. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712
  12. Skjeldal L, Markley JL, Coghlan VM, Vickery LE: 1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins. Biochemistry. 1991 Sep 17;30(37):9078-83. 1909889
  13. Strushkevich N, MacKenzie F, Cherkesova T, Grabovec I, Usanov S, Park HW: Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10139-43. doi: 10.1073/pnas.1019441108. Epub 2011 Jun 2. 21636783