Accession | TIGR00718 |
Name | sda_alpha |
Function | L-serine dehydratase, iron-sulfur-dependent, alpha subunit |
Gene Symbol | sdaAA |
Trusted Cutoff | 243.20 |
Domain Trusted Cutoff | 243.20 |
Noise Cutoff | 201.50 |
Domain Noise Cutoff | 201.50 |
Isology Type | equivalog |
EC Number | 4.3.1.17 |
HMM Length | 300 |
Mainrole Category | Energy metabolism |
Subrole Category | Amino acids and amines |
Gene Ontology Term | GO:0003941: L-serine ammonia-lyase activity molecular_function |
| GO:0006094: gluconeogenesis biological_process |
| GO:0006565: L-serine catabolic process biological_process |
Author | Haft DH |
Entry Date | Feb 1 2000 10:52AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This enzyme is also called serine deaminase. L-serine dehydratase converts serine into pyruvate in the gluconeogenesis pathway from serine. This model describes the alpha chain of an iron-sulfur-dependent L-serine dehydratase, found in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of alpha chains from the homologous region of single chain forms such as found in Escherichia coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. |
References | DR EXPERIMENTAL; EGAD|154938|165375; Peptostreptococcus asaccharolyticus
RM 97386436 |