HMM Summary Page: TIGR00518

AccessionTIGR00518
NamealaDH
Functionalanine dehydrogenase
Gene Symbolald
Trusted Cutoff391.85
Domain Trusted Cutoff391.85
Noise Cutoff173.55
Domain Noise Cutoff173.55
Isology Typeequivalog
EC Number1.4.1.1
HMM Length370
Mainrole CategoryEnergy metabolism
Subrole CategoryAmino acids and amines
Gene Ontology TermGO:0000286: alanine dehydrogenase activity molecular_function
GO:0000286: alanine dehydrogenase activity molecular_function
GO:0000286: alanine dehydrogenase activity molecular_function
GO:0005737: cytoplasm cellular_component
GO:0005737: cytoplasm cellular_component
GO:0005737: cytoplasm cellular_component
GO:0006522: alanine metabolic process biological_process
GO:0006522: alanine metabolic process biological_process
GO:0006522: alanine metabolic process biological_process
AuthorHaft DH
Entry DateOct 18 1999 5:03PM
Last ModifiedFeb 14 2011 3:27PM
CommentThe family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP.
ReferencesDR PFAM; PF01262; AlaDh_PNT; RN [1] RM PMID:11888165 RT Glycine and alanine dehydrogenase activities are catalyzed by the same protein in Mycobacterium smegmatis: upregulation of both activities under microaerophilic adaptation. RA Usha V, Jayaraman R, Toro JC, Hoffner SE, Das KS RL Can J Microbiol. 2002 Jan;48(1):7-13.