SCOPe 2.02: Domain d1llqa1: 1llq A:296-600

Lineage for d1llqa1 (1llq A:296-600)

1. Root: SCOPe 2.02

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.2: NAD(P)-binding Rossmann-fold domains [51734] (1 superfamily)
   core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456
   The nucleotide-binding modes of this and the next two folds/superfamilies are similar

4. Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (13 families)

5. Family c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain [51883] (11 proteins)
   extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site

6. Protein Mitochondrial NAD(P)-dependent malic enzyme [51898] (3 species)
   includes C-terminal additional subdomains

7. Species Pig roundworm (Ascaris suum) [TaxId:6253] [75117] (2 PDB entries)

8. Domain d1llqa1: 1llq A:296-600 [74008]
   Other proteins in same PDB: d1llqa2, d1llqb2
   complexed with nad

Details for d1llqa1

PDB Entry: 1llq, 2.3 Å

PDB Description: Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide

PDB Compounds: (A:) NAD-dependent malic enzyme

SCOPe Domain Sequences for d1llqa1:

Sequence; same for both SEQRES and ATOM records:

>d1llqa1 c.2.1.7 (A:296-600) Mitochondrial NAD(P)-dependent malic enzyme {Pig roundworm (Ascaris suum) [TaxId: 6253]}
iqgtasvivaglltctrvtkklvsqekylffgagaastgiaemivhqmqnegiskeeacn
riylmdidglvtknrkemnprhvqfakdmpettsileviraarpgaligastvrgafnee
viramaeinerpiifalsnptskaectaeeaytftngaalyasgspfpnfelnghtykpg
qgnnayifpgvalgtilfqirhvdndlfllaakkvascvtedslkvgrvypqlkeireis
iqiavemakycykngtanlypqpedlekyvraqvynteyeelinatydwpeqdmrhgfpv
pvvrh

Timeline for d1llqa1:

• d1llqa1 first appeared in SCOP 1.61
  
• d1llqa1 appears in SCOPe 2.01
  
• d1llqa1 appears in SCOPe 2.03
  
• d1llqa1 appears in the current release, SCOPe 2.08