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: waiting to be named.

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 36356: Pyruvate dehydrogenase beta subunit

There are 14 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
Pyruvate dehydrogenase (acetyl-transferring). [EC: 1.2.4.1]
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
  • It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
5374 A0A011SFT9 A0A011SFT9 A0A011U6L9 A0A011U6L9 A0A011UI56 A0A011UI56 A0A013VKC7 A0A013VKC7 A0A017HHZ3 A0A017HHZ3
(5364 more...)
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring). [EC: 1.2.4.4]
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine- residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2).
  • It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2- oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine.
  • It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
  • Formerly EC 1.2.4.3.
2994 A0A011RMU5 A0A011RMU5 A0A023DDF7 A0A023DDF7 A0A023DDZ0 A0A023DDZ0 A0A023PBS5 A0A023PBS5 A0A023PYS7 A0A023PYS7
(2984 more...)
Acetoin dehydrogenase. [EC: 2.3.1.190]
Acetoin + CoA + NAD(+) = acetaldehyde + acetyl-CoA + NADH.
  • This enzyme, which belongs to the family of 2-oxo acid dehydrogenase complexes, catalyzes the oxidative-hydrolytic cleavage of acetoin to acetaldehyde and acetyl-CoA in many bacterial strains, both aerobic and anaerobic.
  • The enzyme is composed of multiple copies of three enzymatic components:acetoin oxidoreductase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3).
74 A0A060UWK7 A0A060UWK7 A0A074INV8 A0A074INV8 A0A087FTH8 A0A087FTH8 A0A098BVQ0 A0A098BVQ0 A0A098FRW1 A0A098FRW1
(64 more...)
Diacetyl reductase ((R)-acetoin forming). [EC: 1.1.1.303]
(R)-acetoin + NAD(+) = diacetyl + NADH.
  • The reaction is catalyzed in the reverse direction.
  • This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).
  • While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible.
  • This enzyme has been reported in the yeast Saccharomyces cerevisiae.
  • Different from EC 1.1.1.304.
  • Formerly EC 1.1.1.5.
72 A0A024DE18 A0A024DE18 A0A081QCM1 A0A081QCM1 A0A0B7GNH5 A0A0B7GNH5 A0A0F2E5G5 A0A0F2E5G5 A0A0F5MKI4 A0A0F5MKI4
(62 more...)
2-oxoisovalerate dehydrogenase (acylating). [EC: 1.2.1.25]
3-methyl-2-oxobutanoate + CoA + NAD(+) = 2-methylpropanoyl-CoA + CO(2) + NADH.
  • Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2- oxopentanoate.
44 A0A031WD22 A0A031WD22 A0A077V7B3 A0A077V7B3 A0A0G3VEZ7 A0A0G3VEZ7 A0A0H3MY19 A0A0H3MY19 A0A0U0CSL5 A0A0U0CSL5
(34 more...)
Dihydrolipoyllysine-residue succinyltransferase. [EC: 2.3.1.61]
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine.
  • A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
32 A0A173KRV3 A0A173KRV3 A0A1A0DDJ4 A0A1A0DDJ4 A3SJZ1 A3SJZ1 A3SY38 A3SY38 A3U3M6 A3U3M6
(22 more...)
Sterol 24-C-methyltransferase. [EC: 2.1.1.41]
S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol.
  • Acts on a range of sterols with a 24(25)-double bond in the side chain.
  • While zymosterol is the preferred substrate it also acts on desmosterol, 5-alpha-cholesta-7,24-dien-3-beta-ol, 5-alpha-cholesta- 5,7,24-trien-3-beta-ol, 4-alpha-methylzymosterol and others.
  • S-adenosyl-L-methionine attacks the Si face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
26 A0A093YHD7 A0A093YHD7 A0A093YK43 A0A093YK43 A0A093ZM00 A0A093ZM00 A0A094AN82 A0A094AN82 A0A094B7G5 A0A094B7G5
(16 more...)
Transketolase. [EC: 2.2.1.1]
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
  • Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH.
  • The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
18 A0A062XIW2 A0A062XIW2 A0A0H2ZG31 A0A0H2ZG31 A0A0U5K6C7 A0A0U5K6C7 A0A157VSN7 A0A157VSN7 A0A175CI65 A0A175CI65
(8 more...)
Dihydrolipoyllysine-residue acetyltransferase. [EC: 2.3.1.12]
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine.
  • A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
14 A0A0X8R411 A0A0X8R411 A0A160TQ65 A0A160TQ65 A0A1B9VL41 A0A1B9VL41 A0A1F2YPQ2 A0A1F2YPQ2 A5VG48 A5VG48
(4 more...)
1-deoxy-D-xylulose-5-phosphate synthase. [EC: 2.2.1.7]
Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2).
  • The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.
  • Formerly EC 4.1.3.37.
8 A0A0P8C9Q6 A0A0P8C9Q6 A0A151ABR0 A0A151ABR0 A0A151AHT3 A0A151AHT3 A0A151AIK3 A0A151AIK3
Serine O-acetyltransferase. [EC: 2.3.1.30]
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.
    2 U2XW33 U2XW33
    Dihydrolipoyl dehydrogenase. [EC: 1.8.1.4]
    Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.
    • A component of the multienzyme 2-oxo-acid dehydrogenase complexes.
    • In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups.
    • It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes.
    • Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine.
    • It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate.
    • Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase.
    • The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein.
    • Formerly EC 1.6.4.3.
    2 A0A163LA25 A0A163LA25
    Diacetyl reductase ((S)-acetoin forming). [EC: 1.1.1.304]
    (S)-acetoin + NAD(+) = diacetyl + NADH.
    • The reaction is catalyzed in the reverse direction.
    • This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).
    • While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible.
    • This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae.
    • Different from EC 1.1.1.303.
    • Formerly EC 1.1.1.5.
    2 H6LFN5 H6LFN5
    Transferred entry: 1.3.98.3. [EC: 1.3.99.22]
      2 U2XUX4 U2XUX4