InterPro : IPR001148

Name  Alpha carbonic anhydrase Short Name  Carbonic_anhydrase_a
Type  Domain Description  Carbonic anhydrases (CA: ) are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate [, ]. The alpha-CAs are found predominantly in animals but also in bacteria and green algae. There are at least 15 isoforms found in mammals, which can be subdivided into cytosolic CAs (CA-I, CA-II, CA-III, CA-VII and CA XIII), mitochondrial CAs (CA-VA and CA-VB), secreted CAs (CA-VI), membrane-associated (CA-IV, CA-IX, CA-XII and CA-XIV) and those without CA activity, the CA-related proteins (CA-RP VIII, X and XI).This entry represents a domain characteristic of alpha class carbonic anhydrases. The dominating secondary structure is a 10-stranded, twisted beta-sheet, which divides the molecules into two halves []. Alpha-CAs contain a single zinc atom bound to three conserved histidine residues. The catalytically active group is the zinc-bound water which ionizes to a hydroxide group. In the mechanism of catalysis, nucleophilic attack of CO2 by a zinc-bound hydroxide ion is followed by displacement of the resulting zinc-bound bicarbonate ion by water; subsequent deprotonation regenerates the nucleophilic zinc-bound hydroxide ion [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR018338 Carbonic anhydrase, alpha-class, conserved site Carbonic_anhydrase_a-class_CS Conserved_site

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Hewett-Emmett D Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families. 1996 Mol Phylogenet Evol 5 50-77
Lindskog S Structure and mechanism of carbonic anhydrase. 1997 Pharmacol Ther 74 1-20
Whittington DA Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells. 2001 Proc Natl Acad Sci U S A 98 9545-50
Supuran CT Carbonic anhydrases--an overview. 2008 Curr Pharm Des 14 603-14
Smith KS Prokaryotic carbonic anhydrases. 2000 FEMS Microbiol Rev 24 335-66

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)