Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1dl2a_ All alpha proteins alpha/alpha toroid Seven-hairpin glycosidases Class I alpha-1 2-mannosidase, catalytic domain baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ], baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyClass I alpha-1 2-mannosidase catalytic domain8026004 4001178 SCOP2 (2022-06-29)
ASCOP2 SuperfamilySeven-hairpin glycosidases8038383 3000996 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGlyco_hydro_47e1dl2A1 A: alpha superhelicesX: Repetitive alpha hairpinsH: alpha/alpha toroid (From Topology)T: alpha/alpha toroidF: Glyco_hydro_47ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.50.10.10 Mainly Alpha Alpha/alpha barrel Glycosyltransferase CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01532Glycosyl hydrolase family 47 (Glyco_hydro_47)Glycosyl hydrolase family 47- Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
CLASS I ALPHA-1,2-MANNOSIDASE

InterPro: Protein Family Classification InterPro Database Homepage

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
mannosyl-oligosaccharide 1,2-alpha-mannosidase  M-CSA #19

Class I alpha-1,2-mannosidases are conserved throughout eukaryotic evolution and are members of the glycoside hydrolase family 47. They regulate the maturation of N-glycans during glycoprotein biosynthesis. N-glycan formation begins with the transfer of a preformed oligosaccharide precursor, usually Glc3Man9ClcNac2, to nascent polypeptide chains. The oligosaccharide precursor is then trimmed immediately by alpha-glucosidases and alpha-mannosidases in the endoplasmic reticulum or the golgi apparatus. Besides their importance in N-glycan maturation, endoplasmic reticulum and golgi apparatus processing glycosidases and mannosidases also play a role in protein folding \"quality control\". Trimming of mannose residues in the endoplasmic reticulum acts as a signal to target misfolded glycoproteins for degradation by the proteasome, which ensures only correctly folded proteins are transported to their final destination.

Mannosyl-oligosaccharide 1,2-alpha-mannosidase is the only alpha-mannosidase in Saccharomyces cerevisae and it removes a single mannose residue from Man(9)(GlcNAc)(2) to form Man(8)(GlcNAc)(2) in the endoplasmic reticulum as do equivalent enzymes in higher organisms. Class I enzymes found in the golgi apparatus remove all four linked alpha-mannose residues.

Defined by 4 residues: GLU:A-99 [auth A-132]ARG:A-103 [auth A-136]ASP:A-242 [auth A-275]GLU:A-397 [auth A-435]
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