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Protein

NADPH:adrenodoxin oxidoreductase, mitochondrial

Gene

FDXR

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

Pathwayi: cholesterol metabolism

This protein is involved in the pathway cholesterol metabolism, which is part of Steroid metabolism.
View all proteins of this organism that are known to be involved in the pathway cholesterol metabolism and in Steroid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei49FAD; via amide nitrogen1 Publication1
Binding sitei70FAD1 Publication1
Binding sitei78FAD; via amide nitrogen1 Publication1
Binding sitei114FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei241NADP1 Publication1
Binding sitei399FAD; via amide nitrogen1 Publication1
Binding sitei406NADP; via amide nitrogen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi185 – 188NADP1 Publication4
Nucleotide bindingi229 – 230NADP1 Publication2
Nucleotide bindingi406 – 408FAD1 Publication3

GO - Molecular functioni

  • ferredoxin-NADP+ reductase activity Source: UniProtKB
  • flavin adenine dinucleotide binding Source: UniProtKB
  • NADP binding Source: UniProtKB
  • NADPH-adrenodoxin reductase activity Source: GO_Central

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-UniPathway
  • oxidation-reduction process Source: UniProtKB
  • 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

BRENDAi1.18.1.6. 908.
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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32Mitochondrion3 PublicationsAdd BLAST32
ChainiPRO_000001941933 – 492NADPH:adrenodoxin oxidoreductase, mitochondrialAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei311PhosphoserineBy similarity1
Modified residuei318PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08165.
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 interactors.
STRINGi9913.ENSBTAP00000056258.

Structurei

Secondary structure

1492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 44Combined sources5
Helixi48 – 60Combined sources13
Beta strandi65 – 69Combined sources5
Beta strandi71 – 75Combined sources5
Helixi78 – 81Combined sources4
Helixi88 – 92Combined sources5
Helixi93 – 101Combined sources9
Beta strandi106 – 111Combined sources6
Turni114 – 116Combined sources3
Helixi120 – 126Combined sources7
Beta strandi127 – 132Combined sources6
Turni145 – 148Combined sources4
Beta strandi152 – 154Combined sources3
Helixi155 – 162Combined sources8
Helixi166 – 168Combined sources3
Beta strandi177 – 184Combined sources8
Helixi187 – 197Combined sources11
Helixi200 – 203Combined sources4
Helixi210 – 217Combined sources8
Beta strandi223 – 227Combined sources5
Helixi232 – 234Combined sources3
Helixi239 – 246Combined sources8
Beta strandi251 – 254Combined sources4
Helixi257 – 260Combined sources4
Helixi263 – 266Combined sources4
Turni267 – 269Combined sources3
Helixi272 – 286Combined sources15
Helixi291 – 298Combined sources8
Beta strandi301 – 307Combined sources7
Beta strandi309 – 317Combined sources9
Beta strandi321 – 337Combined sources17
Helixi338 – 340Combined sources3
Beta strandi342 – 353Combined sources12
Beta strandi355 – 359Combined sources5
Turni376 – 379Combined sources4
Beta strandi394 – 396Combined sources3
Helixi399 – 402Combined sources4
Helixi408 – 428Combined sources21
Helixi439 – 449Combined sources11
Helixi456 – 473Combined sources18
Helixi483 – 489Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP08165.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1800. Eukaryota.
COG0493. LUCA.
HOGENOMiHOG000249250.
HOVERGENiHBG002132.
InParanoidiP08165.
KOiK18914.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR021163. Ferredox_Rdtase_adrenod.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000362. FNR. 1 hit.
SUPFAMiSSF51905. SSF51905. 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. AlignAdd to basket

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

        10         20         30         40         50
MAPRCWRWWP WSSWTRTRLP PSRSIQNFGQ HFSTQEQTPQ ICVVGSGPAG
60 70 80 90 100
FYTAQHLLKH HSRAHVDIYE KQLVPFGLVR FGVAPDHPEV KNVINTFTQT
110 120 130 140 150
ARSDRCAFYG NVEVGRDVTV QELQDAYHAV VLSYGAEDHQ ALDIPGEELP
160 170 180 190 200
GVFSARAFVG WYNGLPENRE LAPDLSCDTA VILGQGNVAL DVARILLTPP
210 220 230 240 250
DHLEKTDITE AALGALRQSR VKTVWIVGRR GPLQVAFTIK ELREMIQLPG
260 270 280 290 300
TRPMLDPADF LGLQDRIKEA ARPRKRLMEL LLRTATEKPG VEEAARRASA
310 320 330 340 350
SRAWGLRFFR SPQQVLPSPD GRRAAGIRLA VTRLEGIGEA TRAVPTGDVE
360 370 380 390 400
DLPCGLVLSS IGYKSRPIDP SVPFDPKLGV VPNMEGRVVD VPGLYCSGWV
410 420 430 440 450
KRGPTGVITT TMTDSFLTGQ ILLQDLKAGH LPSGPRPGSA FIKALLDSRG
460 470 480 490
VWPVSFSDWE KLDAEEVSRG QASGKPREKL LDPQEMLRLL GH
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)DescriptionActionsGraphical viewLength
Sequence conflicti42C → S AA sequence (PubMed:3355838).Curated1
Sequence conflicti77G → R in AAA30362 (PubMed:3038094).Curated1
Sequence conflicti81 – 94FGVAP…VKNVI → VWLALTTPRSRMLL (PubMed:3038094).CuratedAdd BLAST14
Sequence conflicti124 – 128QDAYH → RVYRLT in AAA30362 (PubMed:3038094).Curated5
Sequence conflicti268K → R in AAA30362 (PubMed:3038094).Curated1
Sequence conflicti317 – 318PS → RL in AAA30362 (PubMed:3038094).Curated2
Sequence conflicti323 – 333RAAGIRLAVTR → ARRSAWQSPE in AAA30362 (PubMed:3038094).CuratedAdd BLAST11
Sequence conflicti341 – 352TRAVP…DVEDL → HPGSAHWGCGGP in AAA30362 (PubMed:3038094).CuratedAdd BLAST12
Sequence conflicti488 – 489RL → TM AA sequence (PubMed:3355838).Curated2
Sequence conflicti491G → R in AAX46664 (PubMed:16305752).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003415204E → EVLLLCQ in isoform Long. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP08165. 2 interactors.
STRINGi9913.ENSBTAP00000056258.

Proteomic databases

PaxDbiP08165.
PRIDEiP08165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282604.
KEGGibta:282604.

Organism-specific databases

CTDi2232.

Phylogenomic databases

eggNOGiKOG1800. Eukaryota.
COG0493. LUCA.
HOGENOMiHOG000249250.
HOVERGENiHBG002132.
InParanoidiP08165.
KOiK18914.

Enzyme and pathway databases

UniPathwayiUPA00296.
BRENDAi1.18.1.6. 908.
SABIO-RKP08165.

Miscellaneous databases

EvolutionaryTraceiP08165.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR021163. Ferredox_Rdtase_adrenod.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000362. FNR. 1 hit.
SUPFAMiSSF51905. SSF51905. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 159 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

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.