Protein Domain : Carbonic anhydrase superfamily IPR036874

Type	Homologous_superfamily
Description	Carbonic anhydrases ( ) (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate []. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation []. CA has a resolvase-like fold, which has a core structure composed of three layers (alpha/beta/alpha) arranged in mixed β-sheet of five strands where strand 5 is antiparallel to the rest.Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a superfamily distinct from the one which groups the many different forms of eukaryotic CA's (see ). This superfamily also includes the Bacillus subtilis protein YbcF that does not seem to be able to bind zinc, which all carbonic anhydrases are thought to require, and a carbon disulfide hydrolase from acidothermophilic archaeon Acidianus, which has a typical carbonic anhydrase fold and active site but does not use CO(2) as a substrate [].
Short Name	Carbonic_anhydrase_sf