SCOP 1.65: Domain d3reqb1: 3req B:16-475

Lineage for d3reqb1 (3req B:16-475)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 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] (2 proteins)
   the subunits are clearly related but only one (alpha) is active

6. Protein Methylmalonyl-CoA mutase beta subunit, domain 1 [88711] (1 species)
   the subunits are clearly related but only one (alpha) is active

7. Species Propionibacterium freudenreichii, subsp. shermanii [TaxId:1744] [88712] (8 PDB entries)

8. Domain d3reqb1: 3req B:16-475 [29645]
   Other proteins in same PDB: d3reqa1, d3reqa2, d3reqb2
   complexed with aco; mutant

Details for d3reqb1

PDB Entry: 3req, 2.7 Å

PDB Description: methylmalonyl-coa mutase, substrate-free state (poor quality structure)

SCOP Domain Sequences for d3reqb1:

Sequence; same for both SEQRES and ATOM records:

>d3reqb1 c.1.19.1 (B:16-475) Methylmalonyl-CoA mutase beta subunit, domain 1 {Propionibacterium freudenreichii, subsp. shermanii}
ltpttlslagdfpkateeqwerevekvlnrgrppekqltfaeclkrltvhtvdgidivpm
yrpkdapkklgypgvapftrgttvrngdmdawdvralhedpdekftrkaileglergvts
lllrvdpdaiapehldevlsdvllemtkvevfsrydqgaaaealvsvyersdkpakdlal
nlgldpigfaalqgtepdltvlgdwvrrlakfspdsravtidaniyhnagagdvaelawa
latgaeyvralveqgftateafdtinfrvtathdqfltiarlralreawarigevfgvde
dkrgarqnaitswreltredpyvnilrgsiatfsasvggaesittlpftqalglpeddfp
lriarntgivlaeevnigrvndpaggsyyvesltrsladaawkefqeveklggmskavmt
ehvtkvldacnaerakrlanrkqpitavsefpmigarsie

Timeline for d3reqb1:

• d3reqb1 first appeared (with stable ids) in SCOP 1.55
  
• d3reqb1 appears in SCOP 1.63
  
• d3reqb1 appears in SCOP 1.67
  
• d3reqb1 appears in the current release, SCOPe 2.08