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P08165

- ADRO_BOVIN

UniProt

P08165 - ADRO_BOVIN

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Protein
NADPH:adrenodoxin oxidoreductase, mitochondrial
Gene
FDXR, ADXR
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 nitrogen
Binding sitei70 – 701FAD
Binding sitei78 – 781FAD; via amide nitrogen
Binding sitei114 – 1141FAD; via amide nitrogen and carbonyl oxygen
Binding sitei241 – 2411NADP
Binding sitei399 – 3991FAD; via amide nitrogen
Binding sitei406 – 4061NADP; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1884NADP
Nucleotide bindingi229 – 2302NADP
Nucleotide bindingi406 – 4083FAD

GO - Molecular functioni

  1. NADP binding Source: UniProtKB
  2. ferredoxin-NADP+ reductase activity Source: UniProtKB
  3. flavin adenine dinucleotide 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232Mitochondrion3 Publications
Add
BLAST
Chaini33 – 492460NADPH:adrenodoxin oxidoreductase, mitochondrial
PRO_0000019419Add
BLAST

Proteomic databases

PRIDEiP08165.

Interactioni

Subunit structurei

Monomer. Interacts directly with FDX1.

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

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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei204 – 2041E → EVLLLCQ in isoform Long.
VSP_003415

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421C → S AA sequence 1 Publication
Sequence conflicti77 – 771G → R in AAA30362. 1 Publication
Sequence conflicti81 – 9414FGVAP…VKNVI → VWLALTTPRSRMLL1 Publication
Add
BLAST
Sequence conflicti124 – 1285QDAYH → RVYRLT in AAA30362. 1 Publication
Sequence conflicti268 – 2681K → R in AAA30362. 1 Publication
Sequence conflicti317 – 3182PS → RL in AAA30362. 1 Publication
Sequence conflicti323 – 33311RAAGIRLAVTR → ARRSAWQSPE in AAA30362. 1 Publication
Add
BLAST
Sequence conflicti341 – 35212TRAVP…DVEDL → HPGSAHWGCGGP in AAA30362. 1 Publication
Add
BLAST
Sequence conflicti488 – 4892RL → TM AA sequence 1 Publication
Sequence conflicti491 – 4911G → R in AAX46664. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 143 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

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