HMM Summary Page: TIGR01438

Functionthioredoxin and glutathione reductase
Trusted Cutoff475.85
Domain Trusted Cutoff475.85
Noise Cutoff405.50
Domain Noise Cutoff405.50
Isology Typesubfamily
EC Number1.6.4.-
HMM Length485
AuthorHaft DH
Entry DateFeb 6 2002 3:01PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
ReferencesDR EXPERIMENTAL; PIR:S66677; Homo sapiens; selenocysteine-containing thioredoxin reductase DR OUTGROUP; SP|P47791; glutathione reductase RN [1] RM 11259642 RT Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems. RA Sun QA, Kirnarsky L, Sherman S, Gladyshev VN. RL Proc Natl Acad Sci U S A 2001 Mar 27;98(7):3673-8 RN [2] RM 8650234 RT Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. RA Gladyshev VN, Jeang KT, Stadtman TC. RL Proc Natl Acad Sci U S A 1996 Jun 11;93(12):6146-51