Glycoside Hydrolase Family 65

Known Activitiesα,α-trehalase (EC 3.2.1.28); maltose phosphorylase (EC 2.4.1.8); trehalose phosphorylase (EC 2.4.1.64); kojibiose phosphorylase (EC 2.4.1.230); trehalose-6-phosphate phosphorylase (EC 2.4.1.-); nigerose phosphorylase (EC 2.4.1.-)
Mechanism Inverting
ClanGH-L
3D Structure Status( α / α ) 6
Catalytic Nucleophile/Basephosphate for phosphorylases; water for hydrolases
Catalytic Proton DonorGlu
External resourcesCAZypedia; InterPro; PFAM;
Statistics GenBank accession (792); Uniprot accession (430); PDB accession (1); 3D entries (2); cryst (1)
All (701) Archaea (3) Bacteria (634) Eukaryota (62) unclassified (2) Structure (2 - 1 cryst) Characterized (15)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 maltose phosphorylase (MPase) 2.4.1.8 Bacillus sp. RK-1 BAC54904.1 Q84IX5  
 nigerose phosphorylase (Cphy_1874) 2.4.1.- Clostridium phytofermentans ISDg ABX42243.1 A9KT32  
 trehalose phosphorylase (TPase) 2.4.1.64 Geobacillus stearothermophilus SK-1 BAC20640.1 Q8GRC3  
 maltose phosphorylase (MalP;LBA1870) 2.4.1.8 Lactobacillus acidophilus NCFM AAV43670.1
CAN87417.1
   
 maltose phosphorylase 2.4.1.8 Lactobacillus brevis   Q7SIE1 1H54[A]
 maltose phosphorylase 2.4.1.8 Lactobacillus sanfranciscensis DSM 20451(T) CAA11905.1 O87772  
 trehalose-6-phosphate phosphorylase (TrePP;YeeA;L39593;LL0428) 2.4.1.- Lactococcus lactis subsp. lactis Il1403 AAK04526.1
NP_266584.1
Q9CID5.3  
 maltose phosphorylase (MapA) 2.4.1.8 Paenibacillus sp. SH-55 BAD97810.1
BAJ22988.1
Q50LH0  
 trehalose phosphorylase (TreP) 2.4.1.64 Thermoanaerobacter brockii ATCC 35047 AAE18727.1
AAE24711.1
BAB97299.1
Q8L164 cryst
 kojibiose phosphorylase (KojP;KPase) 2.4.1.230 Thermoanaerobacter brockii ATCC 35047 AAE30762.1
BAB97300.1
Q8L163  
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 AN9340.2 (TreA) 3.2.1.28 Aspergillus nidulans FGSC A4 EAA66407.1    
 acid trehalase (Atc1) 3.2.1.28 Candida albicans AAV05390.1    
 acid trehalase (TreA) 3.2.1.28 Emericella nidulans AAB57642.1 P78617  
 acid trehalase (Atm1) 3.2.1.28 Metarhizium acridum CQMA102 ABB51158.1
ABB51159.1
ABO93464.1
   
 acid trehalase (vacuolar) (Ath1;YPR026w;YP9367.06) 3.2.1.28 Saccharomyces cerevisiae S288c CAA58961.1
CAA89280.1
CAA95022.1
NP_015351.1
P48016  

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
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