SCOPe 2.08: Domain d1e43a2: 1e43 A:1-393

Lineage for d1e43a2 (1e43 A:1-393)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.8: (Trans)glycosidases [51445] (15 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (26 proteins)
   members of the family may contain various insert subdomains
   in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain

6. Protein Bacterial alpha-amylase [51447] (10 species)

7. Species Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId:1390] [63903] (4 PDB entries)
   the N-terminal 300 residues are from B. amyloliquefaciens

8. Domain d1e43a2: 1e43 A:1-393 [59218]
   Other proteins in same PDB: d1e43a1
   complexed with ca, na

Details for d1e43a2

PDB Entry: 1e43, 1.7 Å

PDB Description: native structure of chimaeric amylase from b. amyloliquefaciens and b. licheniformis at 1.7a

PDB Compounds: (A:) alpha-amylase

SCOPe Domain Sequences for d1e43a2:

Sequence; same for both SEQRES and ATOM records:

>d1e43a2 c.1.8.1 (A:1-393) Bacterial alpha-amylase {Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId: 1390]}
vngtlmqyfewytpndgqhwkrlqndaehlsdigitavwippaykglsqsdngygpydly
dlgefqqkgtvrtkygtkselqdaigslhsrnvqvygdvvlnhkagadatedvtavevnp
anrnqetseeyqikawtdfrfpgrgntysdfkwhwyhfdgadwdesrkisrifkfrgegk
awdwevssengnydylmyadvdydhpdvvaetkkwgiwyanelsldgfridaakhikfsf
lrdwvqavrqatgkemftvaeywqnnagklenylnktsfnqsvfdvplhfnlqaassqgg
gydmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypq
vfygdmygtkgdsqreipalkhkiepilkarkq

Timeline for d1e43a2:

• d1e43a2 first appeared in SCOP 1.57
  
• d1e43a2 appears in SCOPe 2.07