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0TRXR2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTXNRD2
DescriptionThioredoxin reductase 2, mitochondrial precursor (ec 1.8.1.9) (tr3) (tr-beta) (selenoprotein z) (selz).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (IEP)
0004791 thioredoxin-disulfide reductase activity (ISS)
0000305 response to oxygen radicals (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry describes both class I and class II oxidoreductases. FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase.rypanothione reductase.ipoamide dehydrogenase.ercuric reductase.hioredoxin reductase.lkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases.n particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase.utidaredoxin reductase.erpredoxin reductase.erredoxin-NAD+ reductase components of benzene 1.-dioxygenase.oluene 1.-dioxygenase.hlorobenzene dioxygenase.iphenyl dioxygenase).ADH oxidase and NADH peroxidase . Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites.uggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently . Despite functional similarities.xidoreductases of this family show no sequence similarity with adrenodoxin reductases and flavoprotein pyridine nucleotidecytochrome reductases (FPNCR) . Assuming that disulphide reductase activity emerged later.uring divergent evolution.he family can be referred to as FAD-dependent pyridine nucleotide reductases.ADPNR.To date.D structures of glutathione reductase .hioredoxin reductase .ercuric reductase .ipoamide dehydrogenase .rypanothione reductase and NADH peroxidase have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta fold.ut the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly. By contrast with the FPNCR family.he folds of the FAD- and NAD(P)H-binding domains are similar.uggesting that the domains evolved by gene duplication .
  IPR013027:FAD-dependent pyridine nucleotide-disulphide oxidoreductase
Proteins that transport heavy metals in micro-organisms and mammals share similarities in their sequences and structures. A conserved 30-residue domain has been found in a number of these heavy metal transport or detoxification proteins . The domain.hich has been termed Heavy-Metal-Associated (HMA).ontains two conserved cysteines that are probably involved in metal binding. The HMA domain has been identified in the N-terminal regions of a variety of cation-transporting ATPases (E1-E2 ATPases). In addition.he domain has been found in bacterial mercuric reductase; the copP copper-binding protein of Helicobacter pylori; and in the N-terminal regions of mercuric transport protein periplasmic component (gene merP) and plasmids carried by mercury-resistant Gram-negative bacteria.here it seems to be a mercury scavenger that specifically binds to one Hg(2+) ion.assing this to mercuric reductase via the merT protein.The structure of the mercuric ion-binding protein MerP from Shigellaflexneri has been determined. The fold has been classed as a ferredoxin-likealpha-beta sandwich.aving a beta-alpha beta-beta alpha-beta architecture.ith the two alpha-helices overlaying a four-stranded anti-parallel beta-sheet . Structural differences between the reduced and mercury-bound forms of merP are localised to the metal-binding loop containing the consensus sequence GMTCXXC.he two cysteines of which are involved inbi-coordination of Hg(2+) . Mercuric reductase.hich contains a single copy of the HMA domain.s involved in a specialised system that confers resistance to Hg(2+) on catalysing the reaction:Hg + NADP+ + H+ = Hg2+ + NADPHThe protein functions as a homodimer.ith an FAD flavoprotein; its active site is a redox-active disulphide bond.
  IPR000815:Mercuric reductase
The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazine ring of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step.he reduced disulphide reduces the substrate. On the basis of sequence and structural similarities .NDR can be categorised into 2 groups. Class I includes glutathione reductase.rypanothione reductase.ipoamide dehydrogenase and mercuric reductase. They cover a wide range of catalytic functions: glutathione reductase ensures that the cell has enough reduced glutathione to maintain protein thiol groups in the reduced state ; trypanothione reductase carries out the analogous reaction in trypanosomal cells (trypanothione is an analogue of glutathione) ; lipoamide dehydrogenase.he E3 component of alpha-ketoacid dehydrogenase multienzyme complex.xidises the dihydrolypoyl groups of lipoate acyltransferase.nd so couples glycolysis to the tricarboxylic acid cycle ; and mercuric reductase enables bacteria to detoxify the mercuric ion by reducing it to elemental mercury.hich evaporates from the cell .
  IPR001100:Pyridine nucleotide-disulphide oxidoreductase, class I
This entry describes a small NADH binding domain within a larger FAD binding domain described by . It is found in both class I and class II oxidoreductases. FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase.rypanothione reductase.ipoamide dehydrogenase.ercuric reductase.hioredoxin reductase.lkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases.n particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase.utidaredoxin reductase.erpredoxin reductase.erredoxin-NAD+ reductase components of benzene 1.-dioxygenase.oluene 1.-dioxygenase.hlorobenzene dioxygenase.iphenyl dioxygenase).ADH oxidase and NADH peroxidase . Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites.uggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently . Despite functional similarities.xidoreductases of this family show no sequence similarity with adrenodoxin reductases and flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) . Assuming that disulphide reductase activity emerged later.uring divergent evolution.he family can be referred to as FAD-dependent pyridine nucleotide reductases.ADPNR.To date.D structures of glutathione reductase .hioredoxin reductase .ercuric reductase .ipoamide dehydrogenase .rypanothione reductase and NADH peroxidase have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta fold.ut the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly. By contrast with the FPNCR family.he folds of the FAD- and NAD(P)H-binding domains are similar.uggesting that the domains evolved by gene duplication .
  IPR001327:Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
Proteins containing this domain include both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
  IPR004099:Pyridine nucleotide-disulphide oxidoreductase dimerisation region
This homodimeric.AD-containing member of the pyridine nucleotide disulphide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly.here SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily.ys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-terminal arm of the protein is proposed to allow broad substrate specificity .
  IPR006338:Thioredoxin and glutathione reductase selenoprotein
IPR013027:Pyr_redox_2 
Evalue:-60.6575775146484 
Location:41-365IPR004099:Pyr_redox_dim 
Evalue:-43.3767509460449 
Location:395-508
SequencesProtein: TRXR2_HUMAN (524 aa)
mRNA: NM_006440
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00384
  Level 3 annotation:
    thioredoxin reductase (NADPH)
  Level 2 annotation:
    Pyrimidine metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 96 residues, 18243045-18243330Exon2: 67 residues, 18244562-18244757Exon3: 34 residues, 18245612-18245710Exon4: 26 residues, 18245888-18245960Exon5: 33 residues, 18247701-18247794Exon6: 34 residues, 18248144-18248240Exon7: 47 residues, 18250847-18250984Exon8: 60 residues, 18262929-18263104Exon9: 32 residues, 18265561-18265653Exon10: 8 residues, 18266571-18266591Exon11: 25 residues, 18278899-18278970Exon12: 23 residues, 18282736-18282799Exon13: 28 residues, 18283287-18283366Exon14: 27 residues, 18285665-18285740Exon15: 50 residues, 18286382-18286527Exon16: 21 residues, 18287065-18287122Exon17: 25 residues, 18298552-18298621Exon18: 99 residues, 18309223-18309515Exon19: 2 residues, -Jump to TRXR2_HUMAN  
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Loci Cluster (Details)Loci: 4555 16596905-16637258 ~-40K 24143(BID)(-)Loci: 3295 16973558-16994498 ~-21K 24153(TUBA8)(+)Loci: 4556 17280294-17304066 ~-24K 24158(PRODH)(-)Loci: 4557 17543094-17546285 ~-3K 24164(SLC25A1)(-)Loci: 4558 17698223-17799219 ~-101K 24167(HIRA)(-)Loci: 3296 18081986-18090842 ~-9K 24176(SEPT5)(+)Loci: 4559 18243045-18309515 ~-66K 24188(TXNRD2)(-)Loci: 3297 18309308-18336528 ~-27K 24191(COMT)(+)Loci: 3294 16423182-16453647 ~-30K 24138(SLC25A18)(+)Link out to UCSC