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InterPro: IPR012999 Pyridine nucleotide-disulphide oxidoreductase, class I, active site
Protein matches
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UniProtKB Matches: 4837 proteins |
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Accession
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IPR012999 Pyr_OxRdtase_I_AS |
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Secondary
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IPR001100
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Type
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Active_site |
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Signatures
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InterPro Relationships
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Found in
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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
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR017817 Mycothione reductase
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contain a pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate. On the basis of sequence and structural similarities [1] these enzymes can be classified into two categories. The first category groups together the following enzymes [2, 3, 4, 5]:
- Glutathione reductase (EC:1.8.1.7) (GR).
- Higher eukaryotes thioredoxin reductase (EC:1.8.1.9).
- Trypanothione reductase (EC:1.8.1.12).
- Lipoamide dehydrogenase (EC:1.8.1.4), the E3 component of alpha-ketoacid dehydrogenase complexes.
- Mercuric reductase (EC:1.16.1.1).
The sequence around the two cysteines involved in the redox-active disulphide bond is conserved and can be used as a signature pattern.
Note: In positions 6 and 7 of the pattern all known sequences have Asn-(Val/ Ile) with the exception of GR from plant chloroplasts and from cyanobacteria which have Ile-Arg [6].
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Structural links
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Database links
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Example proteins
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P00390 Glutathione reductase, 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 |
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| IPR012999 |
Pyridine nucleotide-disulphide oxidoreductase, class I, active site |
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| IPR006338 |
Thioredoxin/glutathione reductase selenoprotein |
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| IPR006322 |
Glutathione reductase, animal/bacterial |
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| IPR000815 |
Mercuric reductase |
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| IPR006258 |
Dihydrolipoamide dehydrogenase |
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| IPR004099 |
Pyridine nucleotide-disulphide oxidoreductase, dimerisation |
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| IPR013027 |
FAD-dependent pyridine nucleotide-disulphide oxidoreductase |
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| IPR001327 |
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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Publications
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1.
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Kuriyan J, Krishna TS, Wong L, Guenther B, Pahler A, Williams CH Jr, Model P.
Convergent evolution of similar function in two structurally divergent enzymes.
Nature 352 172-4 1991
[PubMed: 2067578]
http://dx.doi.org/10.1038/352172a0
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2.
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Rice DW, Schulz GE, Guest JR.
Structural relationship between glutathione reductase and lipoamide dehydrogenase.
J. Mol. Biol. 174 483-96 1984
[PubMed: 6546954]
http://dx.doi.org/10.1016/0022-2836(84)90332-2
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3.
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Carothers DJ, Pons G, Patel MS.
Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases.
Arch. Biochem. Biophys. 268 409-25 1989
[PubMed: 2643922]
http://dx.doi.org/10.1016/0003-9861(89)90309-3
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4.
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Walsh C, Bradley M, Nadeau K.
Molecular studies on trypanothione reductase, a target for antiparasitic drugs.
Trends Biochem. Sci. 16 305-9 1991
[PubMed: 1957352]
http://dx.doi.org/10.1016/0968-0004(91)90124-E
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5.
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Gasdaska PY, Gasdaska JR, Cochran S, Powis G.
Cloning and sequencing of a human thioredoxin reductase.
FEBS Lett. 373 5-9 1995
[PubMed: 7589432]
http://dx.doi.org/10.1016/0014-5793(95)01003-W
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6.
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Creissen G, Edwards EA, Enard C, Wellburn A, Mullineaux P.
Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).
Plant J. 2 129-31 1992
[PubMed: 1303792]
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Additional Reading
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Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS.
How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex.
J. Biol. Chem. 281 2006 648-55
[PubMed: 16263718]
http://dx.doi.org/10.1074/jbc.M507850200
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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
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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
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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
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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
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InterPro 23.1
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