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Protein

Adrenodoxin, mitochondrial

Gene

FDX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates 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.2 Publications

Cofactori

[2Fe-2S] cluster2 PublicationsNote: Binds 1 [2Fe-2S] cluster.2 Publications

Redox potential

E0 is -448 mV.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061Iron-sulfur (2Fe-2S)
Metal bindingi112 – 1121Iron-sulfur (2Fe-2S)
Metal bindingi115 – 1151Iron-sulfur (2Fe-2S)
Metal bindingi152 – 1521Iron-sulfur (2Fe-2S)

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: UniProtKB
  • iron ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Electron transport, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
REACT_150128. Electron transport from NADPH to Ferredoxin.
REACT_150353. Mitochondrial iron-sulfur cluster biogenesis.
REACT_268767. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).

Names & Taxonomyi

Protein namesi
Recommended name:
Adrenodoxin, mitochondrial
Alternative name(s):
Adrenal ferredoxin
Ferredoxin-1
Hepatoredoxin
Gene namesi
Name:FDX1
Synonyms:ADX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3638. FDX1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28082.

Chemistry

DrugBankiDB00648. Mitotane.

Polymorphism and mutation databases

BioMutaiFDX1.
DMDMi113471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060MitochondrionAdd
BLAST
Chaini61 – 184124Adrenodoxin, mitochondrialPRO_0000000988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Modified residuei158 – 1581N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP10109.
PaxDbiP10109.
PRIDEiP10109.

PTM databases

PhosphoSiteiP10109.

Expressioni

Tissue specificityi

Highest levels in the adrenal gland (at protein level). Also detected in kidney and testis (at protein level).1 Publication

Gene expression databases

BgeeiP10109.
CleanExiHS_FDX1.
GenevisibleiP10109. HS.

Organism-specific databases

HPAiHPA041630.
HPA062087.

Interactioni

Subunit structurei

Interacts with CYP11A1.2 Publications

Protein-protein interaction databases

BioGridi108521. 6 interactions.
IntActiP10109. 1 interaction.
STRINGi9606.ENSP00000260270.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 726Combined sources
Beta strandi78 – 836Combined sources
Helixi89 – 968Combined sources
Turni101 – 1066Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi116 – 1183Combined sources
Helixi121 – 1244Combined sources
Helixi132 – 1398Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi148 – 1503Combined sources
Helixi151 – 1533Combined sources
Helixi158 – 1603Combined sources
Beta strandi163 – 1664Combined sources
Helixi171 – 1744Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9YX-ray2.10C/D62-175[»]
3N9ZX-ray2.17C/D62-184[»]
3NA0X-ray2.50C/D88-155[»]
3NA1X-ray2.25C/D62-184[»]
3P1MX-ray2.54A/B/C/D/E/F/G/H61-184[»]
ProteinModelPortaliP10109.
SMRiP10109. Positions 64-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 1711052Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0633.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP10109.
OMAiDHIFEKL.
OrthoDBiEOG708W1D.
PhylomeDBiP10109.
TreeFamiTF319845.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10109-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGGARLL RAASAVLGGP AGRWLHHAGS RAGSSGLLRN RGPGGSAEAS
60 70 80 90 100
RSLSVSARAR SSSEDKITVH FINRDGETLT TKGKVGDSLL DVVVENNLDI
110 120 130 140 150
DGFGACEGTL ACSTCHLIFE DHIYEKLDAI TDEENDMLDL AYGLTDRSRL
160 170 180
GCQICLTKSM DNMTVRVPET VADARQSIDV GKTS
Length:184
Mass (Da):19,393
Last modified:July 1, 1989 - v1
Checksum:iA234EC601136C85F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23668 Genomic DNA. Translation: AAA50462.1.
J03548 mRNA. Translation: AAA96806.1.
M18003 mRNA. Translation: AAA76853.1.
M34788 mRNA. Translation: AAA35829.1.
M34786, M34784 Genomic DNA. Translation: AAA35856.1.
M34785, M34783 Genomic DNA. Translation: AAA35855.1.
BT006681 mRNA. Translation: AAP35327.1.
EF444978 Genomic DNA. Translation: ACA05992.1.
BC010284 mRNA. Translation: AAH10284.1.
BC017063 mRNA. Translation: AAH17063.1.
CCDSiCCDS8344.1.
PIRiA31853. AXHU.
RefSeqiNP_004100.1. NM_004109.4.
UniGeneiHs.744.

Genome annotation databases

EnsembliENST00000260270; ENSP00000260270; ENSG00000137714.
GeneIDi2230.
KEGGihsa:2230.
UCSCiuc001pkx.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23668 Genomic DNA. Translation: AAA50462.1.
J03548 mRNA. Translation: AAA96806.1.
M18003 mRNA. Translation: AAA76853.1.
M34788 mRNA. Translation: AAA35829.1.
M34786, M34784 Genomic DNA. Translation: AAA35856.1.
M34785, M34783 Genomic DNA. Translation: AAA35855.1.
BT006681 mRNA. Translation: AAP35327.1.
EF444978 Genomic DNA. Translation: ACA05992.1.
BC010284 mRNA. Translation: AAH10284.1.
BC017063 mRNA. Translation: AAH17063.1.
CCDSiCCDS8344.1.
PIRiA31853. AXHU.
RefSeqiNP_004100.1. NM_004109.4.
UniGeneiHs.744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9YX-ray2.10C/D62-175[»]
3N9ZX-ray2.17C/D62-184[»]
3NA0X-ray2.50C/D88-155[»]
3NA1X-ray2.25C/D62-184[»]
3P1MX-ray2.54A/B/C/D/E/F/G/H61-184[»]
ProteinModelPortaliP10109.
SMRiP10109. Positions 64-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108521. 6 interactions.
IntActiP10109. 1 interaction.
STRINGi9606.ENSP00000260270.

Chemistry

DrugBankiDB00648. Mitotane.

PTM databases

PhosphoSiteiP10109.

Polymorphism and mutation databases

BioMutaiFDX1.
DMDMi113471.

Proteomic databases

MaxQBiP10109.
PaxDbiP10109.
PRIDEiP10109.

Protocols and materials databases

DNASUi2230.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260270; ENSP00000260270; ENSG00000137714.
GeneIDi2230.
KEGGihsa:2230.
UCSCiuc001pkx.3. human.

Organism-specific databases

CTDi2230.
GeneCardsiGC11P110334.
HGNCiHGNC:3638. FDX1.
HPAiHPA041630.
HPA062087.
MIMi103260. gene.
neXtProtiNX_P10109.
PharmGKBiPA28082.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0633.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP10109.
OMAiDHIFEKL.
OrthoDBiEOG708W1D.
PhylomeDBiP10109.
TreeFamiTF319845.

Enzyme and pathway databases

ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
REACT_150128. Electron transport from NADPH to Ferredoxin.
REACT_150353. Mitochondrial iron-sulfur cluster biogenesis.
REACT_268767. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).

Miscellaneous databases

EvolutionaryTraceiP10109.
GeneWikiiAdrenal_ferredoxin.
GenomeRNAii2230.
NextBioi9031.
PROiP10109.
SOURCEiSearch...

Gene expression databases

BgeeiP10109.
CleanExiHS_FDX1.
GenevisibleiP10109. HS.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and structure of the human adrenodoxin gene."
    Chang C.-Y., Wu D.-A., Lai C.-C., Miller W.L., Chung B.-C.
    DNA 7:609-615(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells."
    Picado-Leonard J., Voutilainen R., Kao L.-C., Chung B.-C., Strauss J.F. III, Miller W.L.
    J. Biol. Chem. 263:3240-3244(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning and sequence analysis of human placental ferredoxin."
    Mittal S., Zhu Y.-Z., Vickery L.E.
    Arch. Biochem. Biophys. 264:383-391(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  4. "Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family."
    Chang C.-Y., Wu D.-A., Mohandas T.K., Chung B.-C.
    DNA Cell Biol. 9:205-212(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Placenta.
  8. "Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode."
    Johnson D., Norman S., Tuckey R.C., Martin L.L.
    Bioelectrochemistry 59:41-47(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CYCLIC VOLTAMMETRY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis."
    Sheftel A.D., Stehling O., Pierik A.J., Elsasser H.P., Muhlenhoff U., Webert H., Hobler A., Hannemann F., Bernhardt R., Lill R.
    Proc. Natl. Acad. Sci. U.S.A. 107:11775-11780(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins."
    Skjeldal L., Markley J.L., Coghlan V.M., Vickery L.E.
    Biochemistry 30:9078-9083(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  14. "Crystal structure of human ferredoxin-1 (FDX1) in complex with iron-sulfur cluster."
    Structural genomics consortium (SGC)
    Submitted (NOV-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 61-184 IN COMPLEX WITH IRON-SULFUR CLUSTER, COFACTOR.
  15. "Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system."
    Strushkevich N., MacKenzie F., Cherkesova T., Grabovec I., Usanov S., Park H.W.
    Proc. Natl. Acad. Sci. U.S.A. 108:10139-10143(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 62-175 IN COMPLEX WITH IRON-SULFUR CLUSTER AND CYP11A1, FUNCTION, COFACTOR, INTERACTION WITH CYP11A1.

Entry informationi

Entry nameiADX_HUMAN
AccessioniPrimary (citable) accession number: P10109
Secondary accession number(s): B0YJ14, Q53YD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 24, 2015
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.