HMM Summary Page: TIGR00720

FunctionL-serine ammonia-lyase
Trusted Cutoff345.10
Domain Trusted Cutoff345.10
Noise Cutoff216.25
Domain Noise Cutoff216.25
Isology Typeequivalog
EC Number4.3.1.17
HMM Length450
Mainrole CategoryEnergy metabolism
Subrole CategoryAmino acids and amines
Gene Ontology TermGO:0003941: L-serine ammonia-lyase activity molecular_function
GO:0006094: gluconeogenesis biological_process
GO:0009063: cellular amino acid catabolic process biological_process
AuthorHaft DH
Entry DateFeb 1 2000 10:52AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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.
ReferencesRN [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.