SCOPe 2.08: Domain d1lvla1: 1lvl A:1-150,A:266-335

Lineage for d1lvla1 (1lvl A:1-150,A:266-335)

1. Root: SCOPe 2.08

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

3. Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
   core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (25 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Dihydrolipoamide dehydrogenase, N- and C-terminal domain [418938] (8 species)

7. Species Pseudomonas putida [TaxId:303] [419390] (1 PDB entry)

8. Domain d1lvla1: 1lvl A:1-150,A:266-335 [30567]
   Other proteins in same PDB: d1lvla2, d1lvla3
   complexed with fad, nad
   has additional insertions and/or extensions that are not grouped together

Details for d1lvla1

PDB Entry: 1lvl, 2.45 Å

PDB Description: the refined structure of pseudomonas putida lipoamide dehydrogenase complexed with nad+ at 2.45 angstroms resolution

PDB Compounds: (A:) dihydrolipoamide dehydrogenase

SCOPe Domain Sequences for d1lvla1:

Sequence; same for both SEQRES and ATOM records:

>d1lvla1 c.3.1.5 (A:1-150,A:266-335) Dihydrolipoamide dehydrogenase, N- and C-terminal domain {Pseudomonas putida [TaxId: 303]}
qqtiqttlliigggpggyvaairagqlgiptvlvegqalggtclnigcipskalihvaeq
fhqasrftepsplgisvasprldigqsvawkdgivdrlttgvaallkkhgvkvvhgwakv
ldgkqvevdgqriqcehlllatgsssvelpXrrprtkgfnlecldlkmngaaiaidercq
tsmhnvwaigdvagepmlahramaqgemvaeiiagkarrfe

Timeline for d1lvla1:

• d1lvla1 first appeared (with stable ids) in SCOP 1.55, called d1lvl_1
  
• d1lvla1 appears in SCOPe 2.07