Glycoside Hydrolase Family 99

Known Activitiesglycoprotein endo-α-1,2-mannosidase (EC 3.2.1.130)
Mechanism Retaining
3D Structure Status( β / α ) 8
Catalytic Nucleophile/BaseUnclear, possible neighboring group participation from O2 (after Thompson et al. Proc. Natl. Acad. Sci. USA., 2012, 109, 781-786)
Catalytic Proton DonorGlu (experimental)
NoteCreated after Spiro, Bhoyroo and Spiro (1997) J. Biol. Chem. 272, 29356-29363
External resourcesCAZypedia;
Statistics GenBank accession (83); Uniprot accession (28); PDB accession (8); 3D entries (2); cryst (0)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 endo-α-1,2-mannosidase (BXY_34140) (BxGH99) 3.2.1.130 Bacteriodes xylanisolvens XB1A CBK68409.1 D6D1V7 4AD1
4AD2
4AD3
4AD4
4AD5
 endo-α-1,2-mannosidase (BT3862) (BtGH99) 3.2.1.130 Bacteroides thetaiotaomicron VPI-5482 AAO78967.1
NP_812773.1
  4ACY
4ACZ
4AD0
 endo-α-1,2-mannosidase (Sama99;Sama_0297) 3.2.1.130 Shewanella amazonensis SB2B ABL98508.1 A1S2A2  
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 glycoprotein endo-α-1,2-mannosidase (ManeA) 3.2.1.130 Homo sapiens AAI46672.1
AAI50200.1
AAL07306.1
AAL07307.1
AAQ75077.1
ACH33940.1
BAB14298.1
BAF84629.1
CAD97640.1
CAE12165.1
CAE45927.1
CAH33902.1
CAI17346.1
CAI17347.1
NP_078917.2
A6H8M6
Q5SRI9
 
 endo-α-1,2-mannosidase (Enman) 3.2.1.130 Rattus norvegicus AAB86925.1
AAT44962.1
NP_542963.1
XP_346734.1
Q5GF25  

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.





Last update: 2012-01-31 © Copyright 1998-2012
AFMB - CNRS - Universités Aix-Marseille I & II