Accession | TIGR01435 |
Name | glu_cys_lig_rel |
Function | glutamate--cysteine ligase/glutathione synthase |
Gene Symbol | gshAB |
Trusted Cutoff | 656.00 |
Domain Trusted Cutoff | 656.00 |
Noise Cutoff | 338.35 |
Domain Noise Cutoff | 338.35 |
Isology Type | equivalog |
EC Number | 6.3.2.2 6.3.2.3 |
HMM Length | 719 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Glutathione and analogs |
Gene Ontology Term | GO:0004357: glutamate-cysteine ligase activity molecular_function |
| GO:0004363: glutathione synthase activity molecular_function |
| GO:0006750: glutathione biosynthetic process biological_process |
Author | Haft DH |
Entry Date | Feb 5 2002 12:12PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This model represents a bifunctional protein family for the biosynthesis of glutathione, and perhaps a range of related
gamma-glutamyltripeptides of the form gamma-Glu-Cys-X(aa). The N-terminal region is similar to proteobacterial glutamate-cysteine ligase. The C-terminal region is homologous to cyanophycin synthetase of cyanobacteria and, more distantly, to D-alanine-D-alanine ligases. Members of this HMM family are found in Listeria and Enterococcus, Gram-positive lineages in which glutathione is produced (see PUBMED:8606174), and in Pasteurella multocida, a Proteobacterium. In Clostridium acetobutylicum, adjacent genes include separate proteins rather than a fusion protein. |
References | RN [1]
RM 17123467
RT Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum.
RA Kino K, Kuratsu S, Noguchi A, Kokubo M, Nakazawa Y, Arai T, Yagasaki M, Kirimura K.
RL Biochem Biophys Res Commun. 2007 Jan 12;352(2):351-9.
DR HAMAP; MF_00782; 13 of 13 |
Genome Property | GenProp0030: glutathione biosynthesis (HMM) |
| GenProp0030: glutathione biosynthesis (HMM) |