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CATH Superfamily 3.30.300.30

ANL, C-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_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 16: Fatty-acid-CoA ligase FadD26

There are 2 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
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).
 110 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579 A0A0E8J579
(100 more...)
4-hydroxyphenylalkanoate adenylyltransferase FadD29. [EC: 6.2.1.51]
(1) ATP + 17-(4-hydroxyphenyl)heptadecanoate + holo- [(phenol)carboxyphthiodiolenone synthase] = AMP + diphosphate + 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase]. (2) ATP + 19-(4-hydroxyphenyl)nonadecanoate + holo- [(phenol)carboxyphthiodiolenone synthase] = AMP + diphosphate + 19-(4-hydroxyphenyl)nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase].
  • The mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols.
  • Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to the phenolphthiocerol/phthiocerol polyketide synthase.
  • Formerly EC 2.7.7.94.
 59 A0A045HD85 A0A045HD85 A0A045HD85 A0A045HD85 A0A045HD85 A0A045HD85 A0A0H3LDA2 A0A0H3LDA2 A0A0H3LDA2 A0A0H3LDA2
(49 more...)