HMM Summary Page: TIGR01438
| Accession | TIGR01438 |
| Name | TGR |
| Function | thioredoxin and glutathione reductase |
| Trusted Cutoff | 475.85 |
| Domain Trusted Cutoff | 475.85 |
| Noise Cutoff | 405.50 |
| Domain Noise Cutoff | 405.50 |
| Isology Type | subfamily |
| EC Number | 1.6.4.- |
| HMM Length | 485 |
| Author | Haft DH |
| Entry Date | Feb 6 2002 3:01PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This 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. |
| References | DR 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 |