| Primary Identifier | IPR044725 | Type | Domain |
| Short Name | CBSX3_CBS_dom |
| description | CBS domains are evolutionarily conserved structural domains found in a variety of non functionally-related proteins from all kingdoms of life. These domains pair together to form a intramolecular dimeric structure (CBS pair), termed Bateman domain [, , , ]. CBS domains have been shown to bind mainly ligands with an adenosyl group such as AMP, ATP and S-AdoMet, but may also bind metal ions, or nucleic acids [, ]. Hence, they play an essential role in the regulation of the activities of numerous proteins, and mutations in them are associated with several hereditary diseases [, , ]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl-carrying ligands. The region containing the CBS domains in cystathionine-beta synthase is involved in regulation by S-AdoMet []. CBS domain pairs from AMPK bind AMP or ATP []. The CBS domains from IMPDH, which bind ATP, have shown to have a role in the regulation of adenylate nucleotide synthesis [, ].This entry represents the CBS domain found in bacteria and plants proteins, including mitochondrial CBSX3 from Arabidopsis. CBSX3 interacts with and activates o-type thioredoxin (Trx-o2) Trx-o2, increasing its activity, which is known to play regulatory roles in the electron transport chain (ETC) complex II. This interaction regulates ROS generation in mitochondria and plays a key role in the modulation of plant development and growth [, ]. |
