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InterPro: IPR004099 Pyridine nucleotide-disulphide oxidoreductase, dimerisation

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8409 proteins

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Accession

IPR004099 Pyr_nucl-diS_OxRdtase_dimer

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.30.390.30	Pyr_redox_dim	8200
Pfam	PF02852	Pyr_redox_dim	7584
Signatures in BioMart

InterPro Relationships Help

Parent

IPR016156 FAD/NAD-linked reductase, dimerisation

Found in

IPR000815 Mercuric reductase
IPR001864 Trypanothione reductase
IPR006258 Dihydrolipoamide dehydrogenase
IPR006322 Glutathione reductase, animal/bacterial
IPR006324 Glutathione reductase, plant
IPR006338 Thioredoxin/glutathione reductase selenoprotein
IPR011796 Mercuric reductase MerA
IPR015723 Glutathione reductase
IPR017758 Coenzyme A disulphide reductase
IPR017817 Mycothione reductase

GO Term annotation Help

Process

GO:0045454 cell redox homeostasis
GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity
GO:0050660 FAD binding

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a dimerisation domain that is usually found at the C-terminal of both class I and class II oxidoreductases, as well as in NADH oxidases and peroxidases [1, 2, 3].

Structural links Help

PDB - click here

SCOP: c.3.1.5 , d.87.1.1 , j.61.1.1

CATH: 3.30.390.30 , 3.50.50.60

Database links Help

Enzyme: EC:1

PANDIT: PF02852

Blocks: IPB004099

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004099

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O95831 Apoptosis-inducing factor 1, mitochondrial

P09624 Dihydrolipoyl dehydrogenase, mitochondrial

P30635 Probable glutathione reductase 2

P91938 Thioredoxin reductase 1, mitochondrial

Q9JLT4 Thioredoxin reductase 2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016156	FAD/NAD-linked reductase, dimerisation
IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site
IPR006338	Thioredoxin/glutathione reductase selenoprotein
IPR000815	Mercuric reductase
IPR006258	Dihydrolipoamide dehydrogenase
IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Mande SS, Parsonage D, Claiborne A, Hol WG. Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303. Biochemistry 34 6985-92 1995 [PubMed: 7766608] http://dx.doi.org/10.1021/bi00021a010
2.	Senda T, Yamada T, Sakurai N, Kubota M, Nishizaki T, Masai E, Fukuda M, Mitsuidagger Y. Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase. J. Mol. Biol. 304 397-410 2000 [PubMed: 11090282] http://dx.doi.org/10.1006/jmbi.2000.4200
3.	Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW. Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Biochemistry 41 12907-13 2002 [PubMed: 12390015] http://dx.doi.org/10.1021/bi026580p

Additional Reading Open in usermanual
	Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN. The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Protein Sci. 5 1996 52-61 [PubMed: 8771196] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8771196
	Urig S, Fritz-Wolf K, Reau R, Herold-Mende C, Toth K, Davioud-Charvet E, Becker K. Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases. Angew. Chem. Int. Ed. Engl. 45 2006 1881-6 [PubMed: 16493712] http://dx.doi.org/10.1002/anie.200502756
	Fritz-Wolf K, Urig S, Becker K. The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis. J. Mol. Biol. 370 2007 116-27 [PubMed: 17512005] http://dx.doi.org/10.1016/j.jmb.2007.04.044
	Yu J, Zhou CZ. Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae. Proteins 68 2007 972-9 [PubMed: 17554778] http://dx.doi.org/10.1002/prot.21354
	Eckenroth BE, Rould MA, Hondal RJ, Everse SJ. Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases. Biochemistry 46 2007 4694-705 [PubMed: 17385893] http://dx.doi.org/10.1021/bi602394p
	Senda M, Kishigami S, Kimura S, Fukuda M, Ishida T, Senda T. Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin. J. Mol. Biol. 373 2007 382-400 [PubMed: 17850818] http://dx.doi.org/10.1016/j.jmb.2007.08.002

InterPro 23.1