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P08165

- ADRO_BOVIN

UniProt

P08165 - ADRO_BOVIN

Protein

NADPH:adrenodoxin oxidoreductase, mitochondrial

Gene

FDXR

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.

    Catalytic activityi

    2 reduced adrenodoxin + NADP+ = 2 oxidized adrenodoxin + NADPH.1 Publication

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491FAD; via amide nitrogen1 Publication
    Binding sitei70 – 701FAD1 Publication
    Binding sitei78 – 781FAD; via amide nitrogen1 Publication
    Binding sitei114 – 1141FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei241 – 2411NADP1 Publication
    Binding sitei399 – 3991FAD; via amide nitrogen1 Publication
    Binding sitei406 – 4061NADP; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi185 – 1884NADP1 Publication
    Nucleotide bindingi229 – 2302NADP1 Publication
    Nucleotide bindingi406 – 4083FAD1 Publication

    GO - Molecular functioni

    1. ferredoxin-NADP+ reductase activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: UniProtKB
    3. NADP binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    SABIO-RKP08165.
    UniPathwayiUPA00296.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH:adrenodoxin oxidoreductase, mitochondrial (EC:1.18.1.6)
    Short name:
    AR
    Short name:
    Adrenodoxin reductase
    Alternative name(s):
    Ferredoxin--NADP(+) reductase
    Short name:
    Ferredoxin reductase
    Gene namesi
    Name:FDXR
    Synonyms:ADXR
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    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 – 3232Mitochondrion3 PublicationsAdd
    BLAST
    Chaini33 – 492460NADPH:adrenodoxin oxidoreductase, mitochondrialPRO_0000019419Add
    BLAST

    Proteomic databases

    PRIDEiP08165.

    Interactioni

    Subunit structurei

    Monomer. Interacts directly with FDX1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FDX1P002572EBI-593948,EBI-593992
    isiBP0A3E03EBI-593948,EBI-593907From a different organism.

    Protein-protein interaction databases

    IntActiP08165. 2 interactions.

    Structurei

    Secondary structure

    1
    492
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 445
    Helixi48 – 6013
    Beta strandi65 – 695
    Beta strandi71 – 755
    Helixi78 – 814
    Helixi88 – 925
    Helixi93 – 1019
    Beta strandi106 – 1116
    Turni114 – 1163
    Helixi120 – 1267
    Beta strandi127 – 1326
    Turni145 – 1484
    Beta strandi152 – 1543
    Helixi155 – 1628
    Helixi166 – 1683
    Beta strandi177 – 1848
    Helixi187 – 19711
    Helixi200 – 2034
    Helixi210 – 2178
    Beta strandi223 – 2275
    Helixi232 – 2343
    Helixi239 – 2468
    Beta strandi251 – 2544
    Helixi257 – 2604
    Helixi263 – 2664
    Turni267 – 2693
    Helixi272 – 28615
    Helixi291 – 2988
    Beta strandi301 – 3077
    Beta strandi309 – 3179
    Beta strandi321 – 33717
    Helixi338 – 3403
    Beta strandi342 – 35312
    Beta strandi355 – 3595
    Turni376 – 3794
    Beta strandi394 – 3963
    Helixi399 – 4024
    Helixi408 – 42821
    Helixi439 – 44911
    Helixi456 – 47318
    Helixi483 – 4897

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CJCX-ray1.70A33-492[»]
    1E1KX-ray1.95A33-492[»]
    1E1LX-ray2.30A33-492[»]
    1E1MX-ray1.85A33-492[»]
    1E1NX-ray2.40A33-492[»]
    1E6EX-ray2.30A/C33-492[»]
    ProteinModelPortaliP08165.
    SMRiP08165. Positions 36-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08165.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0493.
    HOGENOMiHOG000249250.
    HOVERGENiHBG002132.
    InParanoidiP08165.
    KOiK00528.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR021163. Adrenodoxin_Rdtase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PIRSFiPIRSF000362. FNR. 1 hit.

    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 Short (identifier: P08165-1) [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

    MAPRCWRWWP WSSWTRTRLP PSRSIQNFGQ HFSTQEQTPQ ICVVGSGPAG    50
    FYTAQHLLKH HSRAHVDIYE KQLVPFGLVR FGVAPDHPEV KNVINTFTQT 100
    ARSDRCAFYG NVEVGRDVTV QELQDAYHAV VLSYGAEDHQ ALDIPGEELP 150
    GVFSARAFVG WYNGLPENRE LAPDLSCDTA VILGQGNVAL DVARILLTPP 200
    DHLEKTDITE AALGALRQSR VKTVWIVGRR GPLQVAFTIK ELREMIQLPG 250
    TRPMLDPADF LGLQDRIKEA ARPRKRLMEL LLRTATEKPG VEEAARRASA 300
    SRAWGLRFFR SPQQVLPSPD GRRAAGIRLA VTRLEGIGEA TRAVPTGDVE 350
    DLPCGLVLSS IGYKSRPIDP SVPFDPKLGV VPNMEGRVVD VPGLYCSGWV 400
    KRGPTGVITT TMTDSFLTGQ ILLQDLKAGH LPSGPRPGSA FIKALLDSRG 450
    VWPVSFSDWE KLDAEEVSRG QASGKPREKL LDPQEMLRLL GH 492
    Length:492
    Mass (Da):54,338
    Last modified:July 15, 1998 - v3
    Checksum:iE68F6F5D18F53131
    GO
    Isoform Long (identifier: P08165-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         204-204: E → EVLLLCQ

    Note: Represents 10-20% of all adrenodoxin reductase mRNAs and seems to be inactive.

    Show »
    Length:498
    Mass (Da):55,008
    Checksum:iBB3238129E92F3D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421C → S AA sequence (PubMed:3355838)Curated
    Sequence conflicti77 – 771G → R in AAA30362. (PubMed:3038094)Curated
    Sequence conflicti81 – 9414FGVAP…VKNVI → VWLALTTPRSRMLL(PubMed:3038094)CuratedAdd
    BLAST
    Sequence conflicti124 – 1285QDAYH → RVYRLT in AAA30362. (PubMed:3038094)Curated
    Sequence conflicti268 – 2681K → R in AAA30362. (PubMed:3038094)Curated
    Sequence conflicti317 – 3182PS → RL in AAA30362. (PubMed:3038094)Curated
    Sequence conflicti323 – 33311RAAGIRLAVTR → ARRSAWQSPE in AAA30362. (PubMed:3038094)CuratedAdd
    BLAST
    Sequence conflicti341 – 35212TRAVP…DVEDL → HPGSAHWGCGGP in AAA30362. (PubMed:3038094)CuratedAdd
    BLAST
    Sequence conflicti488 – 4892RL → TM AA sequence (PubMed:3355838)Curated
    Sequence conflicti491 – 4911G → R in AAX46664. (PubMed:16305752)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei204 – 2041E → EVLLLCQ in isoform Long. CuratedVSP_003415

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17029 mRNA. Translation: AAA30362.1.
    D00211 mRNA. Translation: BAA00150.1.
    X13736 mRNA. Translation: CAA32002.1.
    D83475 Genomic DNA. Translation: BAA11921.1.
    BT021817 mRNA. Translation: AAX46664.1.
    PIRiJT0751.
    RefSeqiNP_777116.1. NM_174691.1.
    UniGeneiBt.64647.

    Genome annotation databases

    GeneIDi282604.
    KEGGibta:282604.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17029 mRNA. Translation: AAA30362.1 .
    D00211 mRNA. Translation: BAA00150.1 .
    X13736 mRNA. Translation: CAA32002.1 .
    D83475 Genomic DNA. Translation: BAA11921.1 .
    BT021817 mRNA. Translation: AAX46664.1 .
    PIRi JT0751.
    RefSeqi NP_777116.1. NM_174691.1.
    UniGenei Bt.64647.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CJC X-ray 1.70 A 33-492 [» ]
    1E1K X-ray 1.95 A 33-492 [» ]
    1E1L X-ray 2.30 A 33-492 [» ]
    1E1M X-ray 1.85 A 33-492 [» ]
    1E1N X-ray 2.40 A 33-492 [» ]
    1E6E X-ray 2.30 A/C 33-492 [» ]
    ProteinModelPortali P08165.
    SMRi P08165. Positions 36-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08165. 2 interactions.

    Proteomic databases

    PRIDEi P08165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 282604.
    KEGGi bta:282604.

    Organism-specific databases

    CTDi 2232.

    Phylogenomic databases

    eggNOGi COG0493.
    HOGENOMi HOG000249250.
    HOVERGENi HBG002132.
    InParanoidi P08165.
    KOi K00528.

    Enzyme and pathway databases

    UniPathwayi UPA00296 .
    SABIO-RK P08165.

    Miscellaneous databases

    EvolutionaryTracei P08165.
    NextBioi 20806310.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR021163. Adrenodoxin_Rdtase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PIRSFi PIRSF000362. FNR. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of adrenodoxin reductase cDNA from bovine adrenal cortex."
      Sagara Y., Takata Y., Miyata T., Hara T., Horiuchi T.
      J. Biochem. 102:1333-1336(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Molecular cloning and sequence analysis of full-length cDNA for mRNA of adrenodoxin oxidoreductase from bovine adrenal cortex."
      Nonaka Y., Murakami H., Yabusaki Y., Kuramitsu S., Kagamiyama H., Yamano T., Okamoto M.
      Biochem. Biophys. Res. Commun. 145:1239-1247(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases."
      Hanukoglu I., Gutfinger T.
      Eur. J. Biochem. 180:479-484(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adrenal cortex.
    4. "Gene structure of bovine adrenodoxin reductase."
      Takata Y., Sagara Y., Kono A., Sekimizu K., Horiuchi T.
      Biol. Pharm. Bull. 16:1200-1206(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Adrenoferredoxin-binding peptide of NADPH-adrenoferredoxin reductase."
      Hamamoto I., Kurokohchi K., Tanaka S., Ichikawa Y.
      Biochim. Biophys. Acta 953:207-213(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-62; 254-276 AND 487-492.
    7. "Structural and functional characterization of bovine adrenodoxin reductase by limited proteolysis."
      Warburton R.J., Seybert D.W.
      Biochim. Biophys. Acta 1246:39-46(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-51 AND 298-320, CATALYTIC ACTIVITY.
    8. "Isolation of a cDNA for adrenodoxin reductase (ferredoxin-NADP+ reductase). Implications for mitochondrial cytochrome P-450 systems."
      Hanukoglu I., Gutfinger T., Haniu M., Shively J.E.
      Eur. J. Biochem. 169:449-455(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE.
      Tissue: Adrenal cortex.
    9. "The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis."
      Ziegler G.A., Vonrhein C., Hanukoglu I., Schulz G.E.
      J. Mol. Biol. 289:981-990(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-492 IN COMPLEX WITH FAD.
    10. "Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family."
      Ziegler G.A., Schulz G.E.
      Biochemistry 39:10986-10995(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 33-492 IN COMPLEX WITH NADP.
    11. "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 33-492 IN COMPLEX WITH FDX1.

    Entry informationi

    Entry nameiADRO_BOVIN
    AccessioniPrimary (citable) accession number: P08165
    Secondary accession number(s): Q58CY0, Q95KN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3