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P00257

- ADX_BOVIN

UniProt

P00257 - ADX_BOVIN

Protein

Adrenodoxin, mitochondrial

Gene

FDX1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Cofactori

    Binds 1 2Fe-2S cluster.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi104 – 1041Iron-sulfur (2Fe-2S)
    Metal bindingi110 – 1101Iron-sulfur (2Fe-2S)
    Metal bindingi113 – 1131Iron-sulfur (2Fe-2S)
    Metal bindingi150 – 1501Iron-sulfur (2Fe-2S)

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
    2. electron carrier activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: AgBase
    6. protein homodimerization activity Source: AgBase

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB
    2. hormone biosynthetic process Source: UniProtKB
    3. oxidation-reduction process Source: UniProtKB
    4. steroid biosynthetic process Source: UniProtKB

    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_215986. Mitochondrial iron-sulfur cluster biogenesis.
    REACT_224048. Electron transport from NADPH to Ferredoxin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adrenodoxin, mitochondrial
    Alternative name(s):
    Adrenal ferredoxin
    Ferredoxin-1
    Hepato-ferredoxin
    Gene namesi
    Name:FDX1
    Synonyms:ADX
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 15

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5858MitochondrionAdd
    BLAST
    Chaini59 – 186128Adrenodoxin, mitochondrialPRO_0000000986Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
    Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
    Modified residuei156 – 1561N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Interacts with CYP11A1.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FDXRP081652EBI-593992,EBI-593948

    Protein-protein interaction databases

    IntActiP00257. 2 interactions.

    Structurei

    Secondary structure

    1
    186
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi64 – 707
    Beta strandi72 – 743
    Beta strandi76 – 827
    Helixi87 – 937
    Turni99 – 1046
    Beta strandi105 – 1117
    Beta strandi114 – 1163
    Helixi119 – 1224
    Helixi130 – 1367
    Beta strandi143 – 1453
    Beta strandi146 – 1483
    Helixi149 – 1513
    Helixi156 – 1583
    Beta strandi161 – 1644
    Helixi171 – 1733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYFX-ray1.85A/B62-166[»]
    1CJEX-ray2.50A/B/C/D60-186[»]
    1E6EX-ray2.30B/D59-186[»]
    1L6UNMR-A59-186[»]
    1L6VNMR-A59-186[»]
    2BT6X-ray1.50A/B63-166[»]
    2JQRNMR-B62-166[»]
    ProteinModelPortaliP00257.
    SMRiP00257. Positions 63-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00257.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 1691052Fe-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.
    InParanoidiP00257.
    OMAiLLMTIQC.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00257-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAARLLRVAS AALGDTAGRW RLLARPRAGA GGLRGSRGPG LGGGAVATRT    50
    LSVSGRAQSS SEDKITVHFI NRDGETLTTK GKIGDSLLDV VVQNNLDIDG 100
    FGACEGTLAC STCHLIFEQH IFEKLEAITD EENDMLDLAY GLTDRSRLGC 150
    QICLTKAMDN MTVRVPDAVS DARESIDMGM NSSKIE 186
    Length:186
    Mass (Da):19,756
    Last modified:July 1, 1989 - v2
    Checksum:iF0F2EE027BFAC371
    GO
    Isoform 2 (identifier: P00257-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         24-60: ARPRAGAGGLRGSRGPGLGGGAVATRTLSVSGRAQSS → LKSSQFIKVSCSGSWISAAQRAFICYSKSGNITCFLR

    Show »
    Length:186
    Mass (Da):20,395
    Checksum:i7D3E98D62C9D12D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61L → M in AAI09850. 1 PublicationCurated
    Sequence conflicti24 – 241A → V in AAA30357. (PubMed:2994043)Curated
    Sequence conflicti62 – 621E → Q AA sequence (PubMed:4686920)Curated
    Sequence conflicti130 – 1301D → N AA sequence (PubMed:4686920)Curated
    Sequence conflicti134 – 1341D → N AA sequence (PubMed:4686920)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei24 – 6037ARPRA…RAQSS → LKSSQFIKVSCSGSWISAAQ RAFICYSKSGNITCFLR in isoform 2. 1 PublicationVSP_016558Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11746 mRNA. Translation: AAA30357.1.
    M16934 mRNA. Translation: AAA30358.1.
    D00467 mRNA. Translation: BAA00362.1.
    D00471 Genomic DNA. Translation: BAA00363.1.
    M19656, M19474 Genomic DNA. Translation: AAA78950.1.
    BT030601 mRNA. Translation: ABQ13041.1.
    BC109849 mRNA. Translation: AAI09850.1.
    S78831 mRNA. Translation: AAB21264.1.
    PIRiJX0094. AXBO.
    RefSeqiNP_851354.1. NM_181011.2. [P00257-2]
    UniGeneiBt.1573.

    Genome annotation databases

    EnsembliENSBTAT00000015660; ENSBTAP00000015660; ENSBTAG00000011793. [P00257-1]
    GeneIDi281157.
    KEGGibta:281157.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11746 mRNA. Translation: AAA30357.1 .
    M16934 mRNA. Translation: AAA30358.1 .
    D00467 mRNA. Translation: BAA00362.1 .
    D00471 Genomic DNA. Translation: BAA00363.1 .
    M19656 , M19474 Genomic DNA. Translation: AAA78950.1 .
    BT030601 mRNA. Translation: ABQ13041.1 .
    BC109849 mRNA. Translation: AAI09850.1 .
    S78831 mRNA. Translation: AAB21264.1 .
    PIRi JX0094. AXBO.
    RefSeqi NP_851354.1. NM_181011.2. [P00257-2 ]
    UniGenei Bt.1573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYF X-ray 1.85 A/B 62-166 [» ]
    1CJE X-ray 2.50 A/B/C/D 60-186 [» ]
    1E6E X-ray 2.30 B/D 59-186 [» ]
    1L6U NMR - A 59-186 [» ]
    1L6V NMR - A 59-186 [» ]
    2BT6 X-ray 1.50 A/B 63-166 [» ]
    2JQR NMR - B 62-166 [» ]
    ProteinModelPortali P00257.
    SMRi P00257. Positions 63-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00257. 2 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000015660 ; ENSBTAP00000015660 ; ENSBTAG00000011793 . [P00257-1 ]
    GeneIDi 281157.
    KEGGi bta:281157.

    Organism-specific databases

    CTDi 2230.

    Phylogenomic databases

    eggNOGi COG0633.
    GeneTreei ENSGT00530000063577.
    HOGENOMi HOG000244518.
    HOVERGENi HBG000092.
    InParanoidi P00257.
    OMAi LLMTIQC.
    TreeFami TF319845.

    Enzyme and pathway databases

    Reactomei REACT_215986. Mitochondrial iron-sulfur cluster biogenesis.
    REACT_224048. Electron transport from NADPH to Ferredoxin.

    Miscellaneous databases

    EvolutionaryTracei P00257.
    NextBioi 20805220.

    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. "Molecular cloning and amino acid sequence of the precursor form of bovine adrenodoxin: evidence for a previously unidentified COOH-terminal peptide."
      Okamura T., John M.E., Zuber M.X., Simpson E.R., Waterman M.R.
      Proc. Natl. Acad. Sci. U.S.A. 82:5705-5709(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Multiple species of bovine adrenodoxin mRNA. Occurrence of two different mitochondrial precursor sequences associated with the same mature sequence."
      Okamura T., Kagimoto M., Simpson E.R., Waterman M.R.
      J. Biol. Chem. 262:10335-10338(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Structural organization of the bovine adrenodoxin gene."
      Sagara Y., Sawae H., Kimura A., Sagara-Nakano Y., Morohashi K., Miyoshi K., Horiuchi T.
      J. Biochem. 107:77-83(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    4. "Molecular cloning and nucleotide sequences of bovine hepato-ferredoxin cDNA; identical primary structures of hepato- and adreno-ferredoxins."
      Matsuo Y., Tomita S., Tsuneoka Y., Furukawa A., Ichikawa Y.
      Int. J. Biochem. 24:289-295(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. NIH - Mammalian Gene Collection (MGC) project
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: Crossbred X Angus.
      Tissue: Liver.
    7. "Transcription of the bovine adrenodoxin gene produces two species of mRNA of which only one is translated into adrenodoxin."
      Kagimoto M., Kagimoto K., Simpson E.R., Waterman M.R.
      J. Biol. Chem. 263:8925-8928(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
    8. "The amino acid sequence of bovine adrenodoxin."
      Tanaka M., Haniu M., Yasunobu K.T., Kimura T.
      J. Biol. Chem. 248:1141-1157(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-172 (ISOFORM 1).
    9. "Isolation and purification of mature bovine adrenocortical ferredoxin with an elongated carboxyl end."
      Sakihama N., Hiwatashi A., Miyatake A., Shin M., Ichikawa Y.
      Arch. Biochem. Biophys. 264:23-29(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 171-185.
    10. "Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis."
      Mueller J.J., Lapko A., Bourenkov G., Ruckpaul K., Heinemann U.
      J. Biol. Chem. 276:2786-2789(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 59-186 IN COMPLEX WITH ADRENODOXIN REDUCTASE.
    11. "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 OF 59-186.
    12. "A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin."
      Beilke D., Weiss R., Loehr F., Pristovsek P., Hannemann F., Bernhardt R., Rueterjans H.
      Biochemistry 41:7969-7978(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 59-186.
    13. "New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)."
      Mueller A., Mueller J.J., Muller Y.A., Uhlmann H., Bernhardt R., Heinemann U.
      Structure 6:269-280(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 63-166.
    14. "The tertiary structure of full-length bovine adrenodoxin suggests functional dimers."
      Pikuleva I.A., Tesh K., Waterman M.R., Kim Y.
      Arch. Biochem. Biophys. 373:44-55(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiADX_BOVIN
    AccessioniPrimary (citable) accession number: P00257
    Secondary accession number(s): A5D9I2
    , P08498, P12713, Q32KZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3