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P10109

- ADX_HUMAN

UniProt

P10109 - ADX_HUMAN

Protein

Adrenodoxin, mitochondrial

Gene

FDX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
    2. electron carrier activity Source: UniProtKB
    3. iron ion binding Source: ProtInc

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB
    2. hormone biosynthetic process Source: UniProtKB
    3. oxidation-reduction process Source: UniProtKB-KW
    4. small molecule metabolic process Source: Reactome
    5. steroid biosynthetic process Source: UniProtKB-KW

    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_150128. Electron transport from NADPH to Ferredoxin.
    REACT_150353. Mitochondrial iron-sulfur cluster biogenesis.

    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: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3638. FDX1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28082.

    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.
    GenevestigatoriP10109.

    Organism-specific databases

    HPAiHPA041630.

    Interactioni

    Subunit structurei

    Interacts with CYP11A1.2 Publications

    Protein-protein interaction databases

    BioGridi108521. 5 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 – 726
    Beta strandi78 – 836
    Helixi89 – 968
    Turni101 – 1066
    Beta strandi108 – 1114
    Beta strandi116 – 1183
    Helixi121 – 1244
    Helixi132 – 1398
    Beta strandi141 – 1433
    Beta strandi148 – 1503
    Helixi151 – 1533
    Helixi158 – 1603
    Beta strandi163 – 1664
    Helixi171 – 1744

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000244518.
    HOVERGENiHBG000092.
    InParanoidiP10109.
    OMAiARQSVDM.
    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

    MAAAGGARLL RAASAVLGGP AGRWLHHAGS RAGSSGLLRN RGPGGSAEAS    50
    RSLSVSARAR SSSEDKITVH FINRDGETLT TKGKVGDSLL DVVVENNLDI 100
    DGFGACEGTL ACSTCHLIFE DHIYEKLDAI TDEENDMLDL AYGLTDRSRL 150
    GCQICLTKSM DNMTVRVPET VADARQSIDV GKTS 184
    Length:184
    Mass (Da):19,393
    Last modified:July 1, 1989 - v1
    Checksum:iA234EC601136C85F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi113471.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8344.1.
    PIRi A31853. AXHU.
    RefSeqi NP_004100.1. NM_004109.4.
    UniGenei Hs.744.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3N9Y X-ray 2.10 C/D 62-175 [» ]
    3N9Z X-ray 2.17 C/D 62-184 [» ]
    3NA0 X-ray 2.50 C/D 88-155 [» ]
    3NA1 X-ray 2.25 C/D 62-184 [» ]
    3P1M X-ray 2.54 A/B/C/D/E/F/G/H 61-184 [» ]
    ProteinModelPortali P10109.
    SMRi P10109. Positions 64-184.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108521. 5 interactions.
    IntActi P10109. 1 interaction.
    STRINGi 9606.ENSP00000260270.

    Chemistry

    DrugBanki DB00648. Mitotane.

    PTM databases

    PhosphoSitei P10109.

    Polymorphism databases

    DMDMi 113471.

    Proteomic databases

    MaxQBi P10109.
    PaxDbi P10109.
    PRIDEi P10109.

    Protocols and materials databases

    DNASUi 2230.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260270 ; ENSP00000260270 ; ENSG00000137714 .
    GeneIDi 2230.
    KEGGi hsa:2230.
    UCSCi uc001pkx.3. human.

    Organism-specific databases

    CTDi 2230.
    GeneCardsi GC11P110334.
    HGNCi HGNC:3638. FDX1.
    HPAi HPA041630.
    MIMi 103260. gene.
    neXtProti NX_P10109.
    PharmGKBi PA28082.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0633.
    HOGENOMi HOG000244518.
    HOVERGENi HBG000092.
    InParanoidi P10109.
    OMAi ARQSVDM.
    OrthoDBi EOG708W1D.
    PhylomeDBi P10109.
    TreeFami TF319845.

    Enzyme and pathway databases

    Reactomei REACT_150128. Electron transport from NADPH to Ferredoxin.
    REACT_150353. Mitochondrial iron-sulfur cluster biogenesis.

    Miscellaneous databases

    EvolutionaryTracei P10109.
    GeneWikii Adrenal_ferredoxin.
    GenomeRNAii 2230.
    NextBioi 9031.
    PROi P10109.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10109.
    CleanExi HS_FDX1.
    Genevestigatori P10109.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 2Fe-2S_ferredoxin-type.
    IPR001055. Adrenodoxin.
    IPR018298. Adrenodoxin_Fe-S_BS.
    IPR012675. Beta-grasp_dom.
    [Graphical view ]
    Pfami PF00111. Fer2. 1 hit.
    [Graphical view ]
    PRINTSi PR00355. ADRENODOXIN.
    SUPFAMi SSF54292. SSF54292. 1 hit.
    PROSITEi PS51085. 2FE2S_FER_2. 1 hit.
    PS00814. ADX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    13. "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.
    14. "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: October 1, 2014
    This is version 149 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