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Mannose-6-phosphate isomerase, cupin domain
This domain is found in Mannose-6-phosphate isomerase from Archaeoglobus fulgidus (MPI) and similar bacterial sequences. This enzyme catalyses the interconversion of mannose 6-phosphate and fructose 6-phosphate [1,2]. This entry represents the C-terminal domain, which is found associated with PFam:PF20511. This domain shows an all-beta structure. Paper describing PDB structure 2wfp. [1]. 19564693. Structures of mannose-6-phosphate isomerase from Salmonella typhimurium bound to metal atoms and substrate: implications for catalytic mechanism. Sagurthi SR, Gowda G, Savithri HS, Murthy MR;. Acta Crystallogr D Biol Crystallogr. 2009;65:724-732. Paper describing PDB structure 5zt4. [2]. 31063150. Structural and functional insights into phosphomannose isomerase: the role of zinc and catalytic residues. Bangera M, Gowda K G, Sagurthi SR, Murthy MRN;. Acta Crystallogr D Struct Biol. 2019;75:475-487. (from Pfam)
type I phosphomannose isomerase catalytic subunit
This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation [1]. [1]. 8612079. The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. Cleasby A, Wonacott A, Skarzynski T, Hubbard RE, Davies GJ, Proudfoot AE, Bernard AR, Payton MA, Wells TN;. Nat Struct Biol 1996;3:470-479. (from Pfam)
class I mannose-6-phosphate isomerase
mannose-6-phosphate isomerase, class I, catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins
mannose-6-phosphate isomerase, class I
The names phosphomannose isomerase and mannose-6-phosphate isomerase are synonomous. This family contains two rather deeply branched groups. One group contains an experimentally determined phosphomannose isomerase of Streptococcus mutans as well as three uncharacterized paralogous proteins of Bacillus subtilis, all at more than 50 % identity to each other, plus a more distant homolog from Archaeoglobus fulgidus. The other group contains members from E. coli, budding yeast, Borrelia burgdorferi, etc.
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