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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

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:

"
NAD(P)-binding Rossmann-like Domain
".

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 292115: Acyl-CoA synthetase (NDP forming)

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
Acetate--CoA ligase (ADP-forming). [EC: 6.2.1.13]
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA.
  • Also acts on propanoate and, very slowly, on butanoate.
 310 A0A024KIS4 A0A024KIS4 A0A027TYL6 A0A027TYL6 A0A028ASA8 A0A028ASA8 A0A028E2Y3 A0A028E2Y3 A0A029HNU7 A0A029HNU7
(300 more...)
Succinate--CoA ligase (ADP-forming). [EC: 6.2.1.5]
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.
    		 144 A0A024V113 A0A024V113 A0A024VJX2 A0A024VJX2 A0A024VYC9 A0A024VYC9 A0A024WJN5 A0A024WJN5 A0A060RZY4 A0A060RZY4
    (134 more...)
    6-carboxyhexanoate--CoA ligase. [EC: 6.2.1.14]
    ATP + 6-carboxyhexanoate + CoA = AMP + diphosphate + 6-carboxyhexanoyl- CoA.
      		 20 A0A132HKJ7 A0A132HKJ7 A0A1K0IGD3 A0A1K0IGD3 D5RQX6 D5RQX6 F6IEG6 F6IEG6 F8GUZ2 F8GUZ2
      (10 more...)
      Long-chain-fatty-acid--CoA ligase. [EC: 6.2.1.3]
      ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
      • Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity.
      • The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24).
      		 8 A9EVP6 A9EVP6 D5HB62 D5HB62 F4N4K6 F4N4K6 Q5NY39 Q5NY39
      Acetate--CoA ligase. [EC: 6.2.1.1]
      ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
      • Also acts on propanoate and propenoate.
      		 4 A0A0H4KX18 A0A0H4KX18 A0A0P7ZIK2 A0A0P7ZIK2
      Succinate--CoA ligase (GDP-forming). [EC: 6.2.1.4]
      GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.
      • Itaconate can act instead of succinate and ITP instead of GTP.
      		 4 A0A0S1XCH9 A0A0S1XCH9 F0LHG4 F0LHG4
      Mycothiol synthase. [EC: 2.3.1.189]
      Desacetylmycothiol + acetyl-CoA = CoA + mycothiol.
      • This enzyme catalyzes the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium.
      • The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs).
      • The enzyme has been purified from Mycobacterium tuberculosis H37Rv.
      • Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate.
      		 2 A0A0B5FHC2 A0A0B5FHC2
      N-acetylmuramoyl-L-alanine amidase. [EC: 3.5.1.28]
      Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
      • Formerly EC 3.4.12.5, EC 3.4.17.7 and EC 3.4.19.10.
      		 2 A0A1I9ZDD4 A0A1I9ZDD4
      3-hydroxyacyl-CoA dehydrogenase. [EC: 1.1.1.35]
      (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
      • Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate.
      • Some enzymes act, more slowly, with NADP(+).
      • Broad specificity to acyl chain-length (cf. EC 1.1.1.211).
      		 2 A6FTU5 A6FTU5