SCOP 1.63: Domain d2reqd1: 2req D:17-475

Lineage for d2reqd1 (2req D:17-475)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 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.1.19: Cobalamin (vitamin B12)-dependent enzymes [51703] (3 families)

5. Family c.1.19.1: Methylmalonyl-CoA mutase, N-terminal (CoA-binding) domain [51704] (1 protein)

6. Protein Methylmalonyl-CoA mutase, alpha and beta subunits [51705] (1 species)
   the subunits are clearly related but only one (alpha) is active

7. Species Propionibacterium freudenreichii, subsp. shermanii [TaxId:1744] [51706] (8 PDB entries)

8. Domain d2reqd1: 2req D:17-475 [29643]
   Other proteins in same PDB: d2reqa2, d2reqb2, d2reqc2, d2reqd2
   complexed with b12, coa; mutant

Details for d2reqd1

PDB Entry: 2req, 2.5 Å

PDB Description: methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state

SCOP Domain Sequences for d2reqd1:

Sequence; same for both SEQRES and ATOM records:

>d2reqd1 c.1.19.1 (D:17-475) Methylmalonyl-CoA mutase, alpha and beta subunits {Propionibacterium freudenreichii, subsp. shermanii}
tpttlslagdfpkateeqwerevekvlnrgrppekqltfaeclkrltvhtvdgidivpmy
rpkdapkklgypgvapftrgttvrngdmdawdvralhedpdekftrkaileglergvtsl
llrvdpdaiapehldevlsdvllemtkvevfsrydqgaaaealvsvyersdkpakdlaln
lgldpigfaalqgtepdltvlgdwvrrlakfspdsravtidaniyhnagagdvaelawal
atgaeyvralveqgftateafdtinfrvtathdqfltiarlralreawarigevfgvded
krgarqnaitswreltredpyvnilrgsiatfsasvggaesittlpftqalglpeddfpl
riarntgivlaeevnigrvndpaggsyyvesltrsladaawkefqeveklggmskavmte
hvtkvldacnaerakrlanrkqpitavsefpmigarsie

Timeline for d2reqd1:

• d2reqd1 first appeared (with stable ids) in SCOP 1.55
  
• d2reqd1 appears in SCOP 1.61
  
• d2reqd1 appears in SCOP 1.65
  
• d2reqd1 appears in the current release, SCOPe 2.08