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Literature summary for 2.3.1.35 extracted from
- DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain (2005), Protein Sci., 14, 1902-1910.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces clavuligerus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the domain 1 of the enzyme has a socalled DOM-fold, which is a structure with crossing loops with a two-layered beta/alpha architecture of particular topology, also found in the L-aminopeptidase D-Ala-esterase/amidase and the molybdenum cofactor-binding domain, structure-function relationship, comparison of sequence basis for the structure by multiple amino acid sequence alignment, overview | Streptomyces clavuligerus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OAT | - |
Streptomyces clavuligerus |
| ornithine acetyltransferase | - |
Streptomyces clavuligerus |
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Release 2023.1 (January 2023)
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