HMM Summary Page: TIGR02456

Functiontrehalose synthase
Gene SymboltreS
Trusted Cutoff678.35
Domain Trusted Cutoff678.35
Noise Cutoff376.75
Domain Noise Cutoff376.75
Isology Typeequivalog_domain
EC Number5.4.99.16
HMM Length539
Mainrole CategoryEnergy metabolism
Subrole CategoryBiosynthesis and degradation of polysaccharides
Gene Ontology TermGO:0005991: trehalose metabolic process biological_process
GO:0047471: maltose alpha-D-glucosyltransferase activity molecular_function
AuthorHaft DH
Entry DateFeb 3 2005 10:44AM
Last ModifiedFeb 14 2011 3:27PM
CommentTrehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor (PMID:15378530).
ReferencesRN [1] RM 8829531 RT Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48. RA Nishimoto T, Nakano M, Nakada T, Chaen H, Fukuda S, Sugimoto T, Kurimoto M, Tsujisaka Y. RL Biosci Biotechnol Biochem. 1996 Apr;60(4):640-4. RN [2] 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. DR EXPERIMENTAL; SP|P72235; Pimelobacter sp. DR EXPERIMENTAL; GB|AAD50660.3; Thermus caldophilus DR EXPERIMENTAL; GB|CAF20645.1; Corynebacterium glutamicum