SCOPe 2.08: Domain d1w2xc1: 1w2x C:1492-1814

Lineage for d1w2xc1 (1w2x C:1492-1814)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (5 families)

5. Family c.14.1.4: Biotin dependent carboxylase carboxyltransferase domain [89572] (9 proteins)
   Pfam PF01039
   the active site is formed by two different homologous subunits or domains of this fold

6. Protein Acetyl-coenzyme A carboxylase, N-terminal domain [418956] (1 species)
   protein duplication: consists of two similar structural domains forming a functional domain of a larger multifunctional enzyme

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [419416] (8 PDB entries)
   Uniprot Q00955

8. Domain d1w2xc1: 1w2x C:1492-1814 [109138]
   Other proteins in same PDB: d1w2xa2, d1w2xb2, d1w2xc2
   complexed with rcp

Details for d1w2xc1

PDB Entry: 1w2x, 2.8 Å

PDB Description: crystal structure of the carboxyltransferase domain of acetyl-coenzyme a carboxylase in complex with cp-640186

PDB Compounds: (C:) acetyl-coa carboxylase

SCOPe Domain Sequences for d1w2xc1:

Sequence; same for both SEQRES and ATOM records:

>d1w2xc1 c.14.1.4 (C:1492-1814) Acetyl-coenzyme A carboxylase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]}
wlqpkrykahlmgttyvydfpelfrqasssqwknfsadvkltddffisneliedengelt
everepganaigmvafkitvktpeyprgrqfvvvanditfkigsfgpqedeffnkvteya
rkrgipriylaansgarigmaeeivplfqvawndaanpdkgfqylyltsegmetlkkfdk
ensvltertvingeerfviktiigsedglgveclrgsgliagatsrayhdiftitlvtcr
svgigaylvrlgqraiqvegqpiiltgapainkmlgrevytsnlqlggtqimynngvshl
tavddlagvekivewmsyvpakr

Timeline for d1w2xc1:

• d1w2xc1 first appeared in SCOP 1.69
  
• d1w2xc1 appears in SCOPe 2.07