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Identification |
HMDB Protein ID
| HMDBP02111 |
Secondary Accession Numbers
| |
Name
| Adrenodoxin, mitochondrial precursor |
Synonyms
|
- Adrenal ferredoxin
- Ferredoxin- 1
- Hepatoredoxin
|
Gene Name
| FDX1 |
Protein Type
| Enzyme |
Biological Properties |
General Function
| Energy production and conversion |
Specific Function
| Participates in the synthesis of thyroid hormones. Transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450 |
Pathways
|
Not Available
|
Reactions
| Not Available |
GO Classification
|
Function |
ion binding |
cation binding |
binding |
transition metal ion binding |
electron transporter activity |
iron ion binding |
transporter activity |
Process |
cellular metabolism |
electron transport |
generation of precursor metabolites and energy |
physiological process |
metabolism |
|
Cellular Location
|
- Secreted
|
Gene Properties |
Chromosome Location
| Chromosome:11 |
Locus
| 11q22 |
SNPs
| FDX1 |
Gene Sequence
|
>555 bp
ATGGCTGCCGCTGGGGGCGCCCGGCTGCTGCGCGCCGCTTCTGCTGTCCTCGGCGGCCCG
GCCGGCCGGTGGCTGCACCACGCTGGGTCCCGCGCTGGATCCAGCGGCCTGCTGAGGAAC
CGGGGGCCGGGCGGTAGCGCGGAGGCGAGCCGGTCGCTGAGCGTGTCGGCGCGGGCCCGG
AGCAGCTCAGAAGATAAAATAACAGTCCACTTTATAAACCGTGATGGTGAAACATTAACA
ACCAAAGGAAAAGTTGGTGATTCTCTGCTAGATGTTGTGGTTGAAAATAATCTAGATATT
GATGGCTTTGGTGCATGTGAGGGAACCCTGGCTTGTTCAACCTGTCACCTCATCTTTGAA
GATCACATATATGAGAAGTTAGATGCAATCACTGATGAGGAGAATGACATGCTCGATCTG
GCATATGGACTAACAGACAGATCACGGTTGGGCTGCCAAATCTGTTTGACAAAATCTATG
GACAATATGACTGTTCGAGTGCCTGAAACAGTGGCTGATGCCAGACAATCCATTGATGTG
GGCAAGACCTCCTGA
|
Protein Properties |
Number of Residues
| 184 |
Molecular Weight
| 19393.0 |
Theoretical pI
| 5.62 |
Pfam Domain Function
|
|
Signals
|
|
Transmembrane Regions
|
Not Available
|
Protein Sequence
|
>Adrenodoxin, mitochondrial precursor
MAAAGGARLLRAASAVLGGPAGRWLHHAGSRAGSSGLLRNRGPGGSAEASRSLSVSARAR
SSSEDKITVHFINRDGETLTTKGKVGDSLLDVVVENNLDIDGFGACEGTLACSTCHLIFE
DHIYEKLDAITDEENDMLDLAYGLTDRSRLGCQICLTKSMDNMTVRVPETVADARQSIDV
GKTS
|
External Links |
GenBank ID Protein
| 557734 |
UniProtKB/Swiss-Prot ID
| P10109 |
UniProtKB/Swiss-Prot Entry Name
| ADX_HUMAN |
PDB IDs
|
Not Available |
GenBank Gene ID
| M23668 |
GeneCard ID
| FDX1 |
GenAtlas ID
| FDX1 |
HGNC ID
| HGNC:3638 |
References |
General References
| - 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. [PubMed:3229285 ]
- 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. [PubMed:3343244 ]
- 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. [PubMed:2969697 ]
- 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. [PubMed:2340092 ]
- Johnson D, Norman S, Tuckey RC, Martin LL: Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode. Bioelectrochemistry. 2003 Apr;59(1-2):41-7. [PubMed:12699818 ]
- 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. [PubMed:1909889 ]
|