Protein Family Models

Urea carboxylase (UC) catalyses a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis [1]. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity[2]. [1]. 9334321. A novel histidine kinase inhibitor regulating development in Bacillus subtilis. Wang L, Grau R, Perego M, Hoch JA;. Genes Dev. 1997;11:2569-2579. [2]. 20884691. Dur3 is the major urea transporter in Candida albicans and is co-regulated with the urea amidolyase Dur1,2. Navarathna DH, Das A, Morschhauser J, Nickerson KW, Roberts DD;. Microbiology. 2011;157:270-279. (from Pfam)

Date:

2024-10-16

biotin-dependent carboxyltransferase family protein similar to allophanate hydrolase subunit 2 and components of urea amidolyase

Date:

2021-01-25

Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This HMM models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins.

Date:

2019-09-10