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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 2: Long-chain fatty acid transport protein 1

There are 3 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).
 3 O14975 O35488 P97524
Cholate--CoA ligase. [EC: 6.2.1.7]
(1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA. (2) ATP + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26- oate + CoA = AMP + diphosphate + (25R)-3-alpha,7-alpha,12-alpha- trihydroxy-5-beta-cholestanoyl-CoA.
  • This membrane-bound enzyme catalyzes the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters.
  • The second step involves EC 2.3.1.65 and converts the acyl-CoA thioester into the corresponding N-acyl amidate by conjugation with glycine or taurine.
  • Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates.
  • Formerly EC 6.2.1.29.
 3 Q4LDG0 Q9ES38 Q9Y2P5
Isopenicillin-N epimerase. [EC: 5.1.1.17]
Isopenicillin N = penicillin N.
  • Epimerization at C-5 of the 5-amino-5-carboxypentanoyl group to form penicillin N is required to make a substrate for EC 1.14.20.1, to produce cephalosporins.
  • Forms part of the penicillin biosynthesis pathway.
 1 Q8J0E9
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