SCOP 1.67: Domain d1on3e2: 1on3 E:261-524

Lineage for d1on3e2 (1on3 E:261-524)

1. Root: SCOP 1.67

2. Class c: Alpha and beta proteins (a/b) [51349] (130 folds)

3. Fold c.14: ClpP/crotonase [52095] (1 superfamily)
   core: 4 turns of (beta-beta-alpha)n superhelix

4. Superfamily c.14.1: ClpP/crotonase [52096] (4 families)

5. Family c.14.1.4: Biotin dependent carboxylase carboxyltransferase domain [89572] (3 proteins)
   the active site is formed by two different homologous subunits or domains of this fold

6. Protein Methylmalonyl-CoA carboxyltransferase (transcarboxylase 12S) [89575] (1 species)

7. Species Propionibacterium freudenreichii [TaxId:1744] [89576] (2 PDB entries)

8. Domain d1on3e2: 1on3 E:261-524 [87116]

Details for d1on3e2

PDB Entry: 1on3, 1.9 Å

PDB Description: Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)

SCOP Domain Sequences for d1on3e2:

Sequence; same for both SEQRES and ATOM records:

>d1on3e2 c.14.1.4 (E:261-524) Methylmalonyl-CoA carboxyltransferase (transcarboxylase 12S) {Propionibacterium freudenreichii}
teeasfvnpnndvspntelrdivpidgkkgydvrdviakivdwgdylevkagyatnlvta
farvngrsvgivanqpsvmsgcldinasdkaaefvnfcdsfniplvqlvdvpgflpgvqq
eyggiirhgakmlyayseatvpkitvvlrkayggsylamcnrdlgadavyawpsaeiavm
gaegaanvifrkeikaaddpdamraekieeyqnafntpyvaaargqvddvidpadtrrki
asalemyatkrqtrpakkhgnfpc

Timeline for d1on3e2:

• d1on3e2 first appeared in SCOP 1.65
  
• d1on3e2 appears in SCOP 1.69
  
• d1on3e2 appears in the current release, SCOPe 2.08