Carbamate kinase (IPR003964)

Short name: Carb_kinase

Overlapping homologous superfamilies

Family relationships



The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes. The three- enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, arginine deiminase, can account for up to 10% of total cell protein [PMID: 9504342].

Carbamate kinase is involved in the last step of the AD pathway, converting carbamoyl phosphate and ADP into ammonia, carbon dioxide and ATP [PMID: 2537202]. The second step of the pathway involves the degradation of L-citrulline to carbamoyl phosphate and L-ornithine, using ornithine carbamoyltransferase [PMID: 9851988].

The crystal structure of Enterococcus faecium carbamate kinase has been determined to 2.8A resolution [PMID: 10211841]. The enzyme exists as a homodimer of two 33kDa subunits. The hallmark of the dimer is a 16-stranded beta-sheet, surrounded by alpha-helices. Each subunit contains an active site within a large crevice.

GO terms

Biological Process

GO:0006525 arginine metabolic process

Molecular Function

GO:0008804 carbamate kinase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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