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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)DescriptionActionsGraphical viewLength
Metal bindingi106Iron-sulfur (2Fe-2S)1
Metal bindingi112Iron-sulfur (2Fe-2S)1
Metal bindingi115Iron-sulfur (2Fe-2S)1
Metal bindingi152Iron-sulfur (2Fe-2S)1

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

ReactomeiR-HSA-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-HSA-196108. Pregnenolone biosynthesis.
R-HSA-211976. Endogenous sterols.
R-HSA-2395516. Electron transport from NADPH to Ferredoxin.
R-HSA-5579026. 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
Proteomesi
  • UP000005640 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

DisGeNETi2230.
OpenTargetsiENSG00000137714.
PharmGKBiPA28082.

Chemistry databases

DrugBankiDB00648. Mitotane.

Polymorphism and mutation databases

BioMutaiFDX1.
DMDMi113471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 60MitochondrionAdd BLAST60
ChainiPRO_000000098861 – 184Adrenodoxin, mitochondrialAdd BLAST124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63PhosphoserineBy similarity1
Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
Modified residuei158N6-succinyllysineBy similarity1
Modified residuei177PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP10109.
MaxQBiP10109.
PaxDbiP10109.
PeptideAtlasiP10109.
PRIDEiP10109.
TopDownProteomicsiP10109.

PTM databases

iPTMnetiP10109.
PhosphoSitePlusiP10109.

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

BgeeiENSG00000137714.
CleanExiHS_FDX1.
GenevisibleiP10109. HS.

Organism-specific databases

HPAiHPA041630.
HPA062087.

Interactioni

Subunit structurei

Interacts with CYP11A1.2 Publications

Protein-protein interaction databases

BioGridi108521. 11 interactors.
IntActiP10109. 8 interactors.
STRINGi9606.ENSP00000260270.

Structurei

Secondary structure

1184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi67 – 72Combined sources6
Beta strandi78 – 83Combined sources6
Helixi89 – 96Combined sources8
Turni101 – 106Combined sources6
Beta strandi108 – 111Combined sources4
Beta strandi116 – 118Combined sources3
Helixi121 – 124Combined sources4
Helixi132 – 139Combined sources8
Beta strandi141 – 143Combined sources3
Beta strandi148 – 150Combined sources3
Helixi151 – 153Combined sources3
Helixi158 – 160Combined sources3
Beta strandi163 – 166Combined sources4
Helixi171 – 174Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini67 – 1712Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST105

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

eggNOGiKOG3309. Eukaryota.
COG0633. LUCA.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP10109.
OMAiICLKKSM.
OrthoDBiEOG091G0MJ2.
PhylomeDBiP10109.
TreeFamiTF319845.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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.4. 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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108521. 11 interactors.
IntActiP10109. 8 interactors.
STRINGi9606.ENSP00000260270.

Chemistry databases

DrugBankiDB00648. Mitotane.

PTM databases

iPTMnetiP10109.
PhosphoSitePlusiP10109.

Polymorphism and mutation databases

BioMutaiFDX1.
DMDMi113471.

Proteomic databases

EPDiP10109.
MaxQBiP10109.
PaxDbiP10109.
PeptideAtlasiP10109.
PRIDEiP10109.
TopDownProteomicsiP10109.

Protocols and materials databases

DNASUi2230.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260270; ENSP00000260270; ENSG00000137714.
GeneIDi2230.
KEGGihsa:2230.
UCSCiuc001pkx.4. human.

Organism-specific databases

CTDi2230.
DisGeNETi2230.
GeneCardsiFDX1.
HGNCiHGNC:3638. FDX1.
HPAiHPA041630.
HPA062087.
MIMi103260. gene.
neXtProtiNX_P10109.
OpenTargetsiENSG00000137714.
PharmGKBiPA28082.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3309. Eukaryota.
COG0633. LUCA.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP10109.
OMAiICLKKSM.
OrthoDBiEOG091G0MJ2.
PhylomeDBiP10109.
TreeFamiTF319845.

Enzyme and pathway databases

ReactomeiR-HSA-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-HSA-196108. Pregnenolone biosynthesis.
R-HSA-211976. Endogenous sterols.
R-HSA-2395516. Electron transport from NADPH to Ferredoxin.
R-HSA-5579026. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000137714.
CleanExiHS_FDX1.
GenevisibleiP10109. HS.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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...

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: November 2, 2016
This is version 170 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

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 one 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.