Protein Family Models

This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain. (from Pfam)

Date:

2024-08-14

This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase, [3], EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43, [1,2], catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterised describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand[4]. [1]. 9689047. Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs. Munster AK, Eckhardt M, Potvin B, Muhlenhoff M, Stanley P, Gerardy-Schahn R;. Proc Natl Acad Sci U S A 1998;95:9140-9145. [2]. 8663048. Purification, cloning, and expression of a cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi. Tullius MV, Munson RS Jr, Wang J, Gibson BW;. J Biol Chem 1996;271:15373-15380. [3]. 7543480. Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12. Strohmaier H, Remler P, Renner W, Hogenauer G;. J Bacteriol 1995;177:4488-4500. [4]. 11577688. Kinetic properties of the acylneuraminate cytidylyltransferase from Pasteurella haemolytica A2. Bravo IG, Barrallo S, Ferrero MA, Rodriguez-Aparicio LB, Martinez-Blanco H, Reglero A;. Biochem J 2001;358:585-598. (from Pfam)

Date:

2024-10-16

This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars. [1]. 9507048. Domain organisation in phosphomannose isomerases (types I and II). Jensen SO, Reeves PR;. Biochim Biophys Acta 1998;1382:5-7. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Members of this family are enzymes which catalyse the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP) [1]. [1]. 10518523. Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol. Rohdich F, Wungsintaweekul J, Fellermeier M, Sagner S, Herz S, Kis K, Eisenreich W, Bacher A, Zenk MH;. Proc Natl Acad Sci U S A. 1999;96:11758-11763. (from Pfam)

Date:

2024-10-16

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase functions as both an uridyltransferase and acetyltransferase, in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc).

Date:

2017-02-03

Catalyzes the acetylation of glucosamine-1-phosphate and uridylation of N-acetylglucosamine-1-phosphate to produce UDP-GlcNAc; function in cell wall synthesis

Gene:

glmU

Date:

2021-08-24

This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes.

Gene:

glmU

Date:

2024-05-15