Protein Family Models

This entry represents a left-handed beta-helix domain found at the C-terminal of Guanosine-diphospho-d-mannose Pyrophosphorylase (GMP) from Thermotoga maritima [1] and as a linker domain in mannose-1-phosphate guanylyltransferases, alginate biosynthesis protein AlgA and xanthan biosynthesis protein XanB, among others, located between the Nucleotidyl transferase domain at the N-terminal (Pfam:PF00483) and the C-terminal isomerase cupin domain (Pfam:PF01050). This domain is composed of an alpha-helix followed by a short left-handed beta-helix. GMP forms a dimer in which two molecules associate through a tail-to-tail arrangement of this domain [1].. Paper describing PDB structure 2x5s. [1]. 20573954. Structural insights into the catalytic mechanism of bacterial guanosine-diphospho-D-mannose pyrophosphorylase and its regulation by divalent ions. Pelissier MC, Lesley SA, Kuhn P, Bourne Y;. J Biol Chem. 2010;285:27468-27476. (from Pfam)

Date:

2024-10-16

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 represents the conserved barrel domain of the 'cupin' superfamily [1] ('cupa' is the Latin term for a small barrel). [1]. 9573603. Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins. Dunwell JM;. Biotechnol Genet Eng Rev 1998;15:1-32. (from Pfam)

Date:

2024-10-16

All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see Pfam:PF00483. [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

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

mannose-1-phosphate guanyltransferase is involved in the biosynthesis of the capsular polysaccharide colanic acid

Date:

2019-06-24

Gene:

cpsB

Date:

2021-11-04

This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal.

Date:

2024-05-14

Gene:

manC

Date:

2019-11-13