Gene Ontology annotation through association of InterPro records with GO terms

Combined Automated Annotation using Multiple IEA Methods

Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine.

The purified Pseudomonas enzyme is a bifunctional arginine/ornithine succinyltransferase and a heterotetramer of two chain types.

"After SDS/PAGE two subunits of 35 kDa and 37 kDa were evident, indicating that the enzyme is a heterotetramer."

PMID:9393691

Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.

Genetic analysis assigns aruF and aruG to the two transferase chains in the aerobic AST pathway.

"the aruF and aruG genes encode the subunits (AruAI and AruAII) of arginine and ornithine N2-succinyltransferases."

file:PSEPK/astA-I/astA-I-uniprot.txt

UniProtKB entry for PSEPK AstA-I

Assigns Q88EI3 to the beta-chain-specific AstA NCBIfam.

"NCBIfam; TIGR03244; arg_catab_AstA; 1."

file:PSEPK/astA-I/astA-I-bioinformatics/RESULTS.md

Reproducible AstA chain sequence comparison

Q88EI3 is beta-like: it is 85.6% identical across aligned residues to P. aeruginosa beta chain P80358 and 38.0% to alpha chain P80357.

"Q88EI3 is therefore beta-like and Q88EI2 is alpha-like."