| Accession | TIGR00720 |
| Name | sda_mono |
| Function | L-serine ammonia-lyase |
| Trusted Cutoff | 345.10 |
| Domain Trusted Cutoff | 345.10 |
| Noise Cutoff | 216.25 |
| Domain Noise Cutoff | 216.25 |
| Isology Type | equivalog |
| EC Number | 4.3.1.17 |
| HMM Length | 450 |
| 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:0009063: cellular amino acid 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 and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. |
| References | RN [1]
RM PMID:8436113
RT Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12.
RA Su H, Moniakis J, Newman EB
RL Eur J Biochem. 1993 Feb 1;211(3):521-7.
RN [2]
RM PMID:15498577
RT The iron-sulfur cluster in the L-serine dehydratase TdcG from Escherichia coli is required for enzyme activity.
RA Burman JD, Harris RL, Hauton KA, Lawson DM, Sawers RG
RL FEBS Lett. 2004 Oct 22;576(3):442-4. |
