Accession | TIGR02457 |
Name | TreS_Cterm |
Function | putative maltokinase |
Trusted Cutoff | 375.05 |
Domain Trusted Cutoff | 375.05 |
Noise Cutoff | 135.95 |
Domain Noise Cutoff | 135.95 |
Isology Type | hypoth_equivalog_domain |
HMM Length | 529 |
Mainrole Category | Energy metabolism |
Subrole Category | Biosynthesis and degradation of polysaccharides |
Gene Ontology Term | GO:0000023: maltose metabolic process biological_process |
| GO:0005991: trehalose metabolic process biological_process |
| GO:0016866: intramolecular transferase activity molecular_function |
Author | Haft DH |
Entry Date | Feb 3 2005 11:05AM |
Last Modified | Jul 11 2012 11:04AM |
Comment | Three pathways for the biosynthesis of trehalose, an osmoprotectant that in some species is also a precursor of certain cell wall glycolipids. Trehalose synthase, TreS, can interconvert maltose and trehalose, but while the equilibrium may favor trehalose, physiological concentrations of trehalose may be much greater than that of maltose and TreS may act largely in its degradation. This model describes a domain found only as a C-terminal fusion to TreS proteins. The most closely related proteins outside this family, Pep2 of Streptomyces coelicolor and Mak1 of Actinoplanes missouriensis, have known maltokinase activity. We suggest this domain acts as a maltokinase and helps drive conversion of trehalose to maltose. |
References | RN [1]
RM 15378530
RT Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase.
RA Jarling M, Cauvet T, Grundmeier M, Kuhnert K, Pape H.
RL J Basic Microbiol. 2004;44(5):360-73. |