| Description | Acetyl coenzyme A (acetyl-CoA) synthetases (ACDs) were first described in Pyrococcus furiosus and then in other Archaea members as the major energy-conserving enzymes. They catalyse the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate and are able to use other substrates such as phenylacetyl-CoA, indoleacetyl-CoA and isobutyryl-CoA, but not succinyl-CoA. They are involved in the conversion of acetyl-CoA to acetate and in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. There are two isoforms ACD I and II which are heterotetramers (alpha2beta2) consisting of two different subunits, alpha and beta [ , , ]. Each ACD is composed of at least five subdomains with variable sequential arrangement, termed "domain shuffling", which confers a very diverse pattern of subdomain organisation within members of the ACD family. This entry represents the C-terminal domain of the Acetate--CoA ligase [ADP-forming] subunit alpha which corresponds to the ligase CoA domain and adopts a flavodoxin fold []. | Name | Ligase-CoA domain |
| Short Name | Ligase_CoA_dom | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
