Accession | TIGR00518 |
Name | alaDH |
Function | alanine dehydrogenase |
Gene Symbol | ald |
Trusted Cutoff | 391.85 |
Domain Trusted Cutoff | 391.85 |
Noise Cutoff | 173.55 |
Domain Noise Cutoff | 173.55 |
Isology Type | equivalog |
EC Number | 1.4.1.1 |
HMM Length | 370 |
Mainrole Category | Energy metabolism |
Subrole Category | Amino acids and amines |
Gene Ontology Term | GO:0000286: alanine dehydrogenase activity molecular_function |
| GO:0005737: cytoplasm cellular_component |
| GO:0006522: alanine metabolic process biological_process |
Author | Haft DH |
Entry Date | Oct 18 1999 5:03PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | The 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. |
References | DR 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. |