Protein Family Models

Date:

2024-08-14

Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines [2]. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. See Pfam:PF00988. The small chain has a GATase domain in the carboxyl terminus. See Pfam:PF00117. The ATP binding domain (this one) has an ATP-grasp fold. [1]. 7915138. Three-dimensional structure of the biotin carboxylase subunit. of acetyl-CoA carboxylase. Waldrop GL, Rayment I, Holden HM;. Biochemistry 1994;33:10249-10256. [2]. 1972379. Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD. Simmer JP, Kelly RE, Rinker AG Jr, Scully JL, Evans DR;. Biol Chem 1990;265:10395-10402. [3]. 10089390. The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution. Thoden JB, Raushel FM, Benning MM, Rayment I, Holden HM;. Acta Crystallogr D Biol Crystallogr 1999;55:8-24. (from Pfam)

Date:

2024-10-16

This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilise ATP others use GTP. [1]. 8144675. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. Wolodko WT, Fraser ME, James MN, Bridger WA;. J Biol Chem 1994;269:10883-10890. (from Pfam)

Date:

2024-10-16

ADP/GDP-forming succinate--CoA ligase subunit beta provides nucleotide specificity and binds the succinate substrate for the succinate--CoA ligase enzyme, which functions in the citric acid cycle (TCA) by coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP

Date:

2023-01-12

This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases HMM (PF00549). The C-terminal half is described by the ATP-grasp HMM (PF02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G

Gene:

sucC

Date:

2024-06-27

Gene:

sucC

Date:

2021-07-22