Aspartate carbamoyltransferase (IPR002082)

Short name: Asp_carbamoyltransf

Overlapping homologous superfamilies

Family relationships


Aspartate carbamoyltransferase (ATCase) catalyses the formation of carbamoyl-aspartate in the pyrimidine biosynthesis pathway, by the association of aspartate and carbamoyl-phosphate. This is the commitment step in the Escherichia coli pathway and is regulated by feedback inhibition by CTP, the final product of the pathway [PMID: 8098212].

The structural organisation of the ATCase protein varies considerably between different organisms. In bacteria such as E. coli, Salmonella typhimurium and Serratia marcescens, the ATCase is a dodecamer of 2 catalytic (c) trimers and 3 regulatory (r) dimers. The catalytic domains are coded for by the pyrB gene [PMID: 3015959], and the regulatory domains by pyrI [PMID: 3722124]. In Gram-positive bacteria such as Bacillus subtilis, ATCase exists as a trimer of catalytic subunits, but unlike in E. coli, it neither contains nor binds to regulatory subunits. In eukaryotes, ATCase is found as a single domain in a multifunctional enzyme that contains activity for glutamine amidotransferase, carbamoylphosphate synthetase, dihydroorotase, and aspartate carbamoyltransferase.

GO terms

Biological Process

GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process

Molecular Function

GO:0004070 aspartate carbamoyltransferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.