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Reviewed, UniProtKB/Swiss-Prot P56522 (ADRO_RAT)

Last modified October 13, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADPH:adrenodoxin oxidoreductase, mitochondrial
      Short name=Adrenodoxin reductase
      Short name=AR
    EC=1.18.1.2
Alternative name(s):
    Ferredoxin--NADP(+) reductase
      Short name=Ferredoxin reductase
Gene names
Name: Fdxr
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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 activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

Cofactor

FAD.

Pathway

Steroid metabolism; cholesterol metabolism.

Subunit structure

Monomer. Interacts directly with FDX1 By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion
Chain35 – 494460NADPH:adrenodoxin oxidoreductase, mitochondrial
PRO_0000019422

Regions

Nucleotide binding187 – 1904NADP By similarity
Nucleotide binding231 – 2322NADP By similarity
Nucleotide binding408 – 4103FAD By similarity

Sites

Binding site511FAD; via amide nitrogen By similarity
Binding site721FAD By similarity
Binding site801FAD; via amide nitrogen By similarity
Binding site1161FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2431NADP By similarity
Binding site4011FAD; via amide nitrogen By similarity
Binding site4081NADP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P56522-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 5F07B37DFAA9525D

FASTA49454,363
        10         20         30         40         50         60 
MAPRCWRWWS WSAWPGVRPL PSRSTPTPGF CKKFSTQETT PQICVVGSGP AGFYTAQHLL 

        70         80         90        100        110        120 
KHHTRAHVDI YEKQLVPFGL VRFGVAPDHP EVKNVINTFT QTARSDRCAF RGNVVVGRDV 

       130        140        150        160        170        180 
SVPELREAYH AVVLSYGAED HQPLEIPGEE LPGVVSARAF VGWYNGLPEN QKLAPDLSCD 

       190        200        210        220        230        240 
TAVILGQGNV ALDVARILLT PPEHLEKTDI TEVALGVLRQ SRVKTVWIVG RRGPLQVAFT 

       250        260        270        280        290        300 
IKELREMIQL PGTQPILDPS DFLGLQDRIK DVPRPRKRLT ELLLRTATEK PGVEEAARRA 

       310        320        330        340        350        360 
LASRAWGLRF FRSPQQVLPT PDGRRVAGIR LAVTRLEGVG ESTRAVPTGD VEDLPCGLLL 

       370        380        390        400        410        420 
SSVGYKSRPI DPSVPFDPKL GIIPNTEGRV VNAPGLYCSG WVKRGPTGVI TTTMTDSFLT 

       430        440        450        460        470        480 
SQVLLKDLKA GLLPSGPRPG YTAIQALLSD RGVRPVSFSD WEKLDAEEVA RGQGTGKPRE 

       490 
KLVDRREMLQ LLGH 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning, overproduction and characterization of rat adrenodoxin reductase."
Sagara Y., Watanabe Y., Kodama H., Aramaki H.
Biochim. Biophys. Acta 1434:284-295(1999) [PubMed: 10525147] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-54.
Strain: Wistar.
Tissue: Adrenal gland.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

D63761 mRNA. Translation: BAA23759.1.
BC088844 mRNA. Translation: AAH88844.1.
IPIIPI00193379.
RefSeqNP_077067.1.
UniGeneRn.10860

3D structure databases

HSSPHSSP built from PDB template 1CJC based on UniProtKB P08165.
SMRP56522. Positions 40-494.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56522.

Genome annotation databases

EnsemblENSRNOT00000004592; ENSRNOP00000004592; ENSRNOG00000003387; Rattus norvegicus. [Genome view]
GeneID79122.
KEGGrno:79122.

Organism-specific databases

CTD79122.
RGD621648. Fdxr.

Phylogenomic databases

HOVERGENP56522.

Enzyme and pathway databases

BRENDA1.18.1.2. 248.

Gene expression databases

ArrayExpressP56522.
GenevestigatorP56522.
GermOnlineENSRNOG00000003387. Rattus norvegicus.

Family and domain databases

InterProIPR000759. Adrndx_reductase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
[Graphical view]
PfamPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00419. ADXRDTASE.
ProtoNetSearch...

Other Resources

NextBio614546.

Entry information

Entry nameADRO_RAT
AccessionPrimary (citable) accession number: P56522
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 13, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents