Structural Classification of Proteins
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Family: Thiolase-related

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: Thiolase-like [53900]
    consists of two similar domains related by pseudo dyad; duplication
    3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32451; strand 5 is antiparallel to the rest
  4. Superfamily: Thiolase-like [53901]
    link to SUPERFAMILY database - Superfamily
  5. Family: Thiolase-related [53902]

Protein Domains:

  1. Thiolase [53903]
    topology of each domain is similar to the first domain of phosphoglucomutase
    1. Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932] [53904] (2) picpic
  2. Biosynthetic thiolase [53905]
    1. Zoogloea ramigera [TaxId: 350] [53906] (12) picpic
      SQ P07097
  3. Beta-ketoacyl-ACP synthase I [53907]
    1. Escherichia coli [TaxId: 562] [53908] (135) picpic
      SQ P14926
  4. Beta-ketoacyl-ACP synthase II [53909]
    1. Escherichia coli [TaxId: 562] [53910] (10) picpic
    2. Synechocystis sp. [TaxId: 1143] [53911] (1) picpic
    3. Thermus thermophilus [TaxId: 274] [89792] (1) picpic
    4. Streptococcus pneumoniae [TaxId: 1313] [89793] (4) picpic
    5. Thale cress (Arabidopsis thaliana), mitochondrial isoform [TaxId: 3702] [117749] (5) picpic
      SQ Q8L3X9
  5. Actinorhodin polyketide putative beta-ketoacyl synthase 1, KasA [110752]
    1. Streptomyces coelicolor [TaxId: 1902] [110753] (1) picpic
      SQ Q02059
  6. Actinorhodin polyketide putative beta-ketoacyl synthase 2, KasB [110754]
    1. Streptomyces coelicolor [TaxId: 1902] [110755] (1) picpic
      SQ Q02062
  7. Fatty oxidation complex beta subunit (3-ketoacyl-CoA thiolase) [110756]
    1. Pseudomonas fragi [TaxId: 296] [110757] (7) picpic
      SQ P28790
  8. Beta-ketoadipyl CoA thiolase [117750]
    1. Thermus thermophilus [TaxId: 274] [117751] (1) picpic
      SQ Q5SJM1

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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