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InterPro: IPR000759 Adrenodoxin reductase

Protein matches Help

UniProtKB

Matches:

3962 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000759 Adrndx_reductase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00419	ADXRDTASE	3962
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006004 Glutamate synthase (NADPH), homotetrameric
IPR006005 Glutamate synthase, NADH/NADPH, small subunit 1
IPR006006 Glutamate synthase, NADH/NADPH, small subunit 2
IPR012142 Tryptophan 2-monooxygenase
IPR012220 Glutamate synthase, eukaryotic
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR014103 Carotene 7,8-desaturase
IPR017701 Putative selenate reductase YgfK

InterPro annotation

Entry Details in BioMart

Abstract

Mitochondrial P450-containing systems comprise 3 components, an FAD-containing flavoprotein NADPH:adrenodoxin reductase (AR); an iron-sulphur protein, adrenodoxin; and P450 [1]. The direction of electron flow is NADPH to AR to adrenodoxin to P450. FAD can be reduced by 2 electrons from NADPH, which are transferred one at a time to adrenodoxin, a one-electron carrier. Both AR and adrenodoxin are soluble proteins located on the matrix side of the inner mitochondrial membrane. Despite functional parallels, AR shows no global similarity either to flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) or to FAD-dependent pyridine nucleotide reductases (FADPNR) [2]. However, BLAST searches reveal local similarity of the N-terminal region of AR to glutamate synthase and NADH peroxidase, especially in the nucleotide-binding regions, suggesting that AR and FADPNR may be distantly related.

Structural links Help

PDB - click here

SCOP: c.3.1.1 , c.3.1.2 , c.4.1.1

CATH: 3.40.50.720 , 3.50.50.60 , 3.90.660.20

Database links Help

Blocks: IPB000759

COMe: PRX000071

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000759

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P22570 NADPH:adrenodoxin oxidoreductase, mitochondrial

P48360 Probable NADPH:adrenodoxin oxidoreductase, mitochondrial

Q18164 Dihydropyrimidine dehydrogenase [NADP+]

Q61578 NADPH:adrenodoxin oxidoreductase, mitochondrial

Q9V3T9 NADPH:adrenodoxin oxidoreductase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR009051	Alpha-helical ferredoxin
IPR017896	4Fe-4S ferredoxin, iron-sulpur binding domain
IPR012285	Fumarate reductase, C-terminal
IPR001450	4Fe-4S ferredoxin, iron-sulphur binding, subgroup
IPR017900	4Fe-4S ferredoxin, iron-sulphur binding, conserved site
IPR016040	NAD(P)-binding domain
IPR012135	Dihydroorotate dehydrogenase, class 1/ 2
IPR005720	Dihydroorotate dehydrogenase, class 1, core
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR000759	Adrenodoxin reductase
IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Hanukoglu I. Steroidogenic enzymes: structure, function, and regulation of expression. J. Steroid Biochem. Mol. Biol. 43 779-804 1992
2.	Hanukoglu I, Gutfinger T. cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. Eur. J. Biochem. 180 479-84 1989 [PubMed: 2924777] http://dx.doi.org/10.1111/j.1432-1033.1989.tb14671.x

Additional Reading Open in usermanual
	Muller JJ, Lapko A, Bourenkov G, Ruckpaul K, Heinemann U. Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. J. Biol. Chem. 276 2001 2786-9 [PubMed: 11053423] http://dx.doi.org/10.1074/jbc.M008501200
	Bossi RT, Aliverti A, Raimondi D, Fischer F, Zanetti G, Ferrari D, Tahallah N, Maier CS, Heck AJ, Rizzi M, Mattevi A. A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase. Biochemistry 41 2002 8807-18 [PubMed: 12102623] http://dx.doi.org/10.1021/bi025858a
	Pennati A, Razeto A, de Rosa M, Pandini V, Vanoni MA, Mattevi A, Coda A, Aliverti A, Zanetti G. Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA. Biochemistry 45 2006 8712-20 [PubMed: 16846214] http://dx.doi.org/10.1021/bi060369m
	Koch M, Breithaupt C, Kiefersauer R, Freigang J, Huber R, Messerschmidt A. Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. EMBO J. 23 2004 1720-8 [PubMed: 15057273] http://dx.doi.org/10.1038/sj.emboj.7600189
	Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y. Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer. J. Biol. Chem. 277 2002 13155-66 [PubMed: 11796730] http://dx.doi.org/10.1074/jbc.M111877200

InterPro 23.1