SCOPe 2.08: Domain d1mo9a1: 1mo9 A:2-192,A:314-383

Lineage for d1mo9a1 (1mo9 A:2-192,A:314-383)

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 NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase, N- and C-terminal domain [418948] (1 species)

7. Species Xanthobacter sp., py2 [TaxId:35809] [419404] (5 PDB entries)

8. Domain d1mo9a1: 1mo9 A:2-192,A:314-383 [79341]
   Other proteins in same PDB: d1mo9a2, d1mo9a3, d1mo9b2, d1mo9b3
   complexed with fad, kpc
   has additional insertions and/or extensions that are not grouped together

Details for d1mo9a1

PDB Entry: 1mo9, 1.65 Å

PDB Description: nadph dependent 2-ketopropyl coenzyme m oxidoreductase/carboxylase complexed with 2-ketopropyl coenzyme m

PDB Compounds: (A:) orf3

SCOPe Domain Sequences for d1mo9a1:

Sequence; same for both SEQRES and ATOM records:

>d1mo9a1 c.3.1.5 (A:2-192,A:314-383) NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase, N- and C-terminal domain {Xanthobacter sp., py2 [TaxId: 35809]}
kvwnarndhltinqwatrideileapdggeviynvdendpreydaifigggaagrfgsay
lramggrqlivdrwpflggscphnacvphhlfsdcaaelmlartfsgqywfpdmtekvvg
ikevvdlfragrngphgimnfqskeqlnleyilncpakvidnhtveaagkvfkaknlila
vgagpgtldvpXeqprsaelakilgldlgpkgevlvneylqtsvpnvyavgdliggpmem
fkarksgcyaarnvmgekisyt

Timeline for d1mo9a1:

• d1mo9a1 first appeared in SCOP 1.63
  
• d1mo9a1 appears in SCOPe 2.07