Glycoside Hydrolase Family 13 / Subf 10

Activities in Sub Family[retaining] α-amylase (EC 3.2.1.1);
[retaining] maltooligosyltrehalose trehalohydrolase (EC 3.2.1.141);
Mechanism Retaining a
ClanGH-H
3D Structure Status( β / α ) 8 barrel
Catalytic Nucleophile/BaseAsp (experimental)
Catalytic Proton DonorGlu (experimental)
NoteNew: many members have been assigned to subfamilies as described by Stam et al. (2006) Protein Eng Des Sel. 19, 555-562 (PMID: 17085431)
External resourcesCAZypedia; EBI Protein of the Month; HOMSTRAD; PDB Molecule of the Month; PRINTS;
Commercial Enzyme Provider(s)MEGAZYME; PROZOMIX;
Statistics GenBank accession (8); Uniprot accession (16); PDB accession (18); 3D entries (3); cryst (0)
Archaea
Protein Name EC# OrganismGenBankUniprot
PDB/3D Carbohydrate Ligands Resolution (Å)
Subf
 α-amylase / maltooligosyltrehalose trehalohydrolase (GTHase) 3.2.1.1
3.2.1.141
Saccharolobus solfataricus KM1 AAR46454.1
BAA11010.1
Q55088
1EH9[A] 3.00
1EHA[A] 3.00
3VGB[A] 2.65
3VGD[A] 2.40
3VGE[A] 2.70
3VGF[A] α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp
2.30
3VGG[A] α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-3)-α-D-Glcp
2.66
3VGH[A] α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-1)-α-D-Glcp
2.60
10
Bacteria
Protein Name EC# OrganismGenBankUniprot
PDB/3D Carbohydrate Ligands Resolution (Å)
Subf
 malto-oligosyltrehalose trehalohydrolase (DrMTHase; DR0464) 3.2.1.141 Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 AAF10042.1
ANC72786.1
NP_294187.1
Q9RX51
2BHU[A] 1.1
2BHY[A] α-D-Glcp
α-D-Glcp-(1-1)-α-D-Glcp
1.5
2BHZ[A] α-D-Glcp-(1-4)-β-D-Glcp
1.2
2BXY[A] α-D-Glcp
α-D-Glcp-(1-1)-α-D-Glcp
β-D-Glcp
1.75
2BXZ[A] α-D-Glcp
α-D-Glcp-(1-1)-α-D-Glcp
β-D-Glcp
1.75
2BY0[A] α-D-Glcp-(1-1)-α-D-Glcp
β-D-Glcp
1.55
2BY1[A] α-D-Glcp-(1-1)-α-D-Glcp
β-D-Glcp
1.55
2BY2[A] α-D-Glcp
α-D-Glcp-(1-1)-α-D-Glcp
β-D-Glcp
1.5
2BY3[A] α-D-Glcp-(1-1)-α-D-Glcp
β-D-Glcp
1.5
10
 STM1560   Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 AAL20478.1
NP_460519.1
 
3M07[A] 1.40
10
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