SCOPe 2.08: Domain d1tkkf1: 1tkk F:126-358

Lineage for d1tkkf1 (1tkk F:126-358)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 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.1.11: Enolase C-terminal domain-like [51604] (3 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this superfamily

5. Family c.1.11.2: D-glucarate dehydratase-like [51609] (15 proteins)

6. Protein L-Ala-D/L-Glu epimerase [69397] (2 species)

7. Species Bacillus subtilis [TaxId:1423] [69399] (2 PDB entries)
   Uniprot O34508

8. Domain d1tkkf1: 1tkk F:126-358 [107099]
   Other proteins in same PDB: d1tkka2, d1tkkb2, d1tkkc2, d1tkkd2, d1tkke2, d1tkkf2, d1tkkg2, d1tkkh2
   complexed with ala, mg

Details for d1tkkf1

PDB Entry: 1tkk, 2.1 Å

PDB Description: The Structure of a Substrate-Liganded Complex of the L-Ala-D/L-Glu Epimerase from Bacillus subtilis

PDB Compounds: (F:) similar to chloromuconate cycloisomerase

SCOPe Domain Sequences for d1tkkf1:

Sequence; same for both SEQRES and ATOM records:

>d1tkkf1 c.1.11.2 (F:126-358) L-Ala-D/L-Glu epimerase {Bacillus subtilis [TaxId: 1423]}
yrdtletdytvsvnspeemaadaenylkqgfqtlkikvgkddiatdiariqeirkrvgsa
vklrldanqgwrpkeavtairkmedaglgielveqpvhkddlaglkkvtdatdtpimade
svftprqafevlqtrsadliniklmkaggisgaekinamaeacgvecmvgsmietklgit
aaahfaaskrnitrfdfdaplmlktdvfnggitysgstismpgkpglgiigaa

Timeline for d1tkkf1:

• d1tkkf1 first appeared in SCOP 1.69
  
• d1tkkf1 appears in SCOPe 2.07