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CATH Superfamily 2.40.110.10

Butyryl-CoA Dehydrogenase, subunit A, domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Butyryl-CoA Dehydrogenase, subunit A, domain 2
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 14322: Isovaleryl-CoA dehydrogenase Butyryl-CoA dehydroge...

There are 9 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Isovaleryl-CoA dehydrogenase. [EC: 1.3.8.4]
Isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein.
  • Pentanoate can act as donor.
  • Formerly EC 1.3.99.10.
 466 A0A009GSJ4 A0A009HF58 A0A009IN59 A0A009K5Z9 A0A009Q0A9 A0A009THK8 A0A010QSJ2 A0A017H8D8 A0A017HKJ3 A0A024HHC4
(456 more...)
Transferred entry: 1.3.8.4. [EC: 1.3.99.10]
    		80 A0A063TRJ9 A0A090IFS2 A0A0C6P6C3 A0A0E9L929 A0A0H3LS32 A0A0H5DIJ7 A0A0N8TX40 A0A0S4WA20 A0A0U2WD54 A0A160SFK9
    (70 more...)
    Short-chain acyl-CoA dehydrogenase. [EC: 1.3.8.1]
    A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
    • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
    • The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms.
    • The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms.
    • The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA.
    • The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA.
    • Cf. EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9.
    • Formerly EC 1.3.2.1 and EC 1.3.99.2.
    		 45 A0A063TRJ9 A0A069PDT0 A0A077JWA3 A0A095K5A9 A0A0C4Y454 A0A0C4YQH9 A0A0C6P6C3 A0A0D6FEX9 A0A0E1AZ64 A0A0E1UNL7
    (35 more...)
    Methylcrotonoyl-CoA carboxylase. [EC: 6.4.1.4]
    ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA.
      		 4 A0A0F4XIL8 G4MDC8 G8PXS5 S6JGV3
      2-methylacyl-CoA dehydrogenase. [EC: 1.3.99.12]
      2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor.
      • Also oxidizes 2-methylpropanoyl-CoA.
      • Not identical with EC 1.3.8.1, EC 1.3.8.7, EC 1.3.8.8 or EC 1.3.8.9.
      		 3 A0A084FW00 A0A137SDC0 Q9FS88
      Catechol 1,2-dioxygenase. [EC: 1.13.11.1]
      Catechol + O(2) = cis,cis-muconate.
      • Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
      • Formerly EC 1.13.1.1 and EC 1.99.2.2.
      		 2 A0A060TC96 A0A0L1HX35
      Medium-chain acyl-CoA dehydrogenase. [EC: 1.3.8.7]
      A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
      • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
      • The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C(8) to C(12) compounds.
      • The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) compounds.
      • cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
      • Formerly EC 1.3.2.2 and EC 1.3.99.3.
      		 1 A0A161MM80
      Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9. [EC: 1.3.99.3]
        		1 D2U865
        Peroxiredoxin. [EC: 1.11.1.15]
        2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
        • Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins.
        • They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins.
        • The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine.
        • All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid).
        • The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes.
        • For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle.
        • In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond.
        • To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor.
        • The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule.
        		 1 A0A0L1HX35
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