Structural Classification of Proteins
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Family: Biotin dependent carboxylase carboxyltransferase domain

Pfam 01039
the active site is formed by two different homologous subunits or domains of this fold

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: ClpP/crotonase [52095]
    core: 4 turns of (beta-beta-alpha)n superhelix
  4. Superfamily: ClpP/crotonase [52096]
    link to SUPERFAMILY database - Superfamily
  5. Family: Biotin dependent carboxylase carboxyltransferase domain [89572]
    Pfam 01039
    the active site is formed by two different homologous subunits or domains of this fold

Protein Domains:

  1. Acetyl-coenzyme A carboxylase [89573]
    duplication: consists of two similar structural domains forming a functional domain of a larger multifunctional enzyme
    1. Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932] [89574] (7) picpic
      SQ Q00955 1482-2196
  2. Methylmalonyl-CoA carboxyltransferase (transcarboxylase 12S) [89575]
    1. Propionibacterium freudenreichii [TaxId: 1744] [89576] (2) picpic
  3. Glutaconyl-CoA decarboxylase A subunit [102210]
    1. Acidaminococcus fermentans [TaxId: 905] [102211] (1) picpic
  4. Propionyl-CoA carboxylase complex B subunit, PccB [117466]
    1. Streptomyces coelicolor [TaxId: 1902] [117467] (4) picpic
      SQ Q9X4K7
    2. Mycobacterium tuberculosis [TaxId: 1773] [142010] (12) picpic
      SQ P96885 20-277! SQ P96885 278-548
    3. Thermotoga maritima [TaxId: 2336] [142011] (12) picpic
      SQ Q9WZH5 1-251! SQ Q9WZH5 252-515
  5. Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, AccA [142012]
    1. Escherichia coli [TaxId: 562] [142013] (1) picpic
      SQ P0ABD5 4-319
  6. Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, AccD [142014]
    1. Escherichia coli [TaxId: 562] [142015] (1) picpic
      SQ P0A9Q6 23-285
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MRC site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk