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CATH Superfamily 3.40.50.620

HUPs

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:

"
HUPs
".

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 85763: Probable cysteine--tRNA ligase, mitochondrial

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
Cysteine--tRNA ligase. [EC: 6.1.1.16]
ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
    		 5 Q2KIF8 Q6DJ95 Q6PA41 Q8BYM8 Q9HA77
    Lipoyl synthase. [EC: 2.8.1.8]
    Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl- L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)- (lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.
    • Member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (i.e. S-adenosylmethionine, or S-(5'-deoxyadenosin- 5'-yl)methionine), by the addition of an electron from an iron-sulfur center.
    • The radical is converted into 5'-deoxyadenosine when it abstracts a hydrogen atom from C-6 and C-8, leaving reactive radicals at these positions so that they can add sulfur, with inversion of configuration.
    • Catalyzes the final step in the de-novo biosynthesis of the lipoyl cofactor, with the other enzyme involved being EC 2.3.1.181.
    • Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein.
    • Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
    • An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs).
    		 1 A0A094FL14
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