Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli.
-
AstC is one of four enzymes with ACOAT activity in arginine synthesis; ArgD is the major one.
"The enzymes with N-acetylornithine aminotransferase (ACOAT) activity in arginine synthesis were ArgD, AstC, GabT and PuuE; the major anaerobic ACOAT was ArgD."
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
-
astC encodes the succinylornithine aminotransferase, the third AST enzyme; its disruption prevents arginine catabolism and impairs ornithine use.
"We identified the E. coli gene for succinylornithine aminotransferase, the third enzyme of the AST pathway, which appears to be the first of an astCADBE operon."
The Escherichia coli starvation gene cstC is involved in amino acid catabolism.
Determination of the structure of the catabolic N-succinylornithine transaminase (AstC) from Escherichia coli.
-
AstC is a dimeric PLP-dependent delta-aminotransferase using succinylornithine and 2-oxoglutarate.
"AstC is a dimeric, pyridoxal phosphate (PLP)-dependent δ–aminotransferase that operates a ping-pong bi-bi reaction mechanism with succinylornithine (SO) and α-ketoglutarate (αKG) as co-substrates and succinylglutamic semialdehyde and glutamate as co-products"
UniProtKB entry P77581 (ASTC_ECOLI)
-
Curated function with secondary acetylornithine activity.
"Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase."