TABLE 2.
Alignment of the generally conserved regions of the α-amylase familya
| Enzyme | Sequenceb in:
|
|||
|---|---|---|---|---|
| Region I | Region II | Region III | Region IV | |
| Acid amylase | LMVDVVPNH | DGLRIDSVLE | YCVGEVDN | NFIENHD |
| AmyA | LMVDVVANH | DGLRIDTVKH | YCIGEVLD | TFVENHD |
| AgtA | LMMDTVINN | DGLRIDAAKH | FMTGEVLQ | SFSENHD |
| AgtB | LLLDVVINN | DGLRIDAAKS | FMTGEVMD | NFIEDQD |
| AgtC | LMLDIVVGD | DGLRIDSVLN | FTVGEGAT | TFTANQD |
| Aah3p (S. pombe) | VMLDSIVNS | DGLRIDAVKM | YSVGEVFS | TFIENHD |
| Amino acid numberingc | 135-143 | 222-231 | 247-254 | 312-318 |
a
Alignment of the generally conserved regions of the α-amylase family as present in A. niger acid amylase and α-amylase AmyA compared to homologous regions in AgtA, AgtB, and AgtC from A. niger and the homologous protein Aah3p from S. pombe.
b
Catalytic residues are underlined, and generally conserved residues are indicated in bold type.
c
Amino acid numbering according to A. niger acid amylase.