SMART: Pro_CA domain annotation

Pro_CA Carbonic anhydrase

SMART accession number:	SM00947
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 (PUBMED:1740425). In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation (PUBMED:1584776). Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.
Interpro abstract (IPR001765):	Carbonic anhydrases (EC 4.2.1.1) (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 [(PUBMED:1740425)]. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation [(PUBMED:1584776)]. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's (see IPR001148). Hypothetical proteins yadF from Escherichia coli and HI1301 from Haemophilus influenzae also belong to this family. This family 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.
GO function:	carbonate dehydratase activity (GO:0004089), zinc ion binding (GO:0008270)
Family alignment:	View or

There are 2076 Pro_CA domains in 2070 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Pro_CA domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Fukuzawa H, Suzuki E, Komukai Y, Miyachi S
- A gene homologous to chloroplast carbonic anhydrase (icfA) is essential tophotosynthetic carbon dioxide fixation by Synechococcus PCC7942.
- Proc Natl Acad Sci U S A. 1992; 89: 4437-41
- Display abstract
- To understand the CO2-concentrating mechanism in cyanobacteria, a genomicDNA fragment that complements a temperature-sensitive high-CO2(5%)-requiring mutant of Synechococcus PCC7942 has been isolated. An openreading frame (ORF272) encoding a polypeptide of 272 amino acids (Mr,30,184) was found within the genomic region located 20 kilobasesdownstream from the genes for ribulose-1,5-bisphosphatecarboxylase/oxygenase (rbcLS). Insertion of a kanamycin-resistance genecartridge within the ORF272 in wild-type cells led to a high-CO2-requiringphenotype. Strains carrying a gene disabled by insertional mutagenesisaccumulated inorganic carbon in the cells, but they could not fix itefficiently, even though ribulose-1,5-bisphosphate carboxylase activitywas comparable to that of the wild-type strain. Therefore, the ORF272 wasdesignated as a gene icfA, which is essential to inorganic carbonfixation. Furthermore, the predicted icfA gene product shared significantsequence similarities with plant chloroplast carbonic anhydrases (CAs)from pea (22%) and spinach (22%) and also with the Escherichia coli cynTgene product (31%), which was recently identified to be E. coli CA. Theseresults indicate that the putative CA encoded by icfA is essential tophotosynthetic carbon dioxide fixation in cyanobacteria and that plantchloroplast CAs may have evolved from a common ancestor of the prokaryoticCAs, which are distinct from mammalian CAs and Chlamydomonas periplasmicCAs.
- Guilloton MB, Korte JJ, Lamblin AF, Fuchs JA, Anderson PM
- Carbonic anhydrase in Escherichia coli. A product of the cyn operon.
- J Biol Chem. 1992; 267: 3731-4
- Display abstract
- The product of the cynT gene of the cyn operon in Escherichia coli hasbeen identified as a carbonic anhydrase. The cyn operon also includes thegene cynS, encoding the enzyme cyanase. Cyanase catalyzes the reaction ofcyanate with bicarbonate to give ammonia and carbon dioxide. The carbonicanhydrase was isolated from an Escherichia coli strain overexpressing thecynT gene and characterized. The purified enzyme was shown to contain 1Zn2+/subunit (24 kDa) and was found to behave as an oligomer in solution;the presence of bicarbonate resulted in partial dissociation of theoligomeric enzyme. The kinetic properties of the enzyme are similar tothose of carbonic anhydrases from other species, including inhibition bysulfonamides and cyanate. The amino acid sequence shows a high degree ofidentity with the sequences of two plant carbonic anhydrases. but not withanimal and algal carbonic anhydrases. Since carbon dioxide formed in thebicarbonate-dependent decomposition of cyanate diffuses out of the cellfaster than it would be hydrated to bicarbonate, the apparent function ofthe induced carbonic anhydrase is to catalyze hydration of carbon dioxideand thus prevent depletion of cellular bicarbonate.
Structure (3D structures containing this domain)

3D Structures of Pro_CA domains in PDB

PDB code	Main view	Title
1ddz		X-ray structure of a beta-carbonic anhydrase from the red alga, porphyridium purpureum r-1
1ekj		The x-ray crystallographic structure of beta carbonic anhydrase from the c3 dicot pisum sativum
1g5c		Crystal structure of the 'cab' type beta class carbonic anhydrase from methanobacterium thermoautotrophicum
1i6o		Crystal structure of e. coli beta carbonic anhydrase (ecca)
1i6p		Crystal structure of e. coli beta carbonic anhydrase (ecca)
1t75		Crystal structure of escherichia coli beta carbonic anhydrase
1ylk		Crystal structure of rv1284 from mycobacterium tuberculosis in complex with thiocyanate
1ym3		Crystal structure of carbonic anhydrase rv3588c from mycobacterium tuberculosis
2a5v		Crystal structure of m. tuberculosis beta carbonic anhydrase, rv3588c, tetrameric form
2a8c		Haemophilus influenzae beta-carbonic anhydrase
2a8d		Haemophilus influenzae beta-carbonic anhydrase complexed with bicarbonate
2esf		Identification of a novel non-catalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase
2w3n		Structure and inhibition of the co2-sensing carbonic anhydrase can2 from the pathogenic fungus cryptococcus neoformans
2w3q		Structure and inhibition of the co2-sensing carbonic anhydrase can2 from the pathogenic fungus cryptococcus neoformans
3e1v		H. influenzae beta-carbonic anhydrase, variant d44n
3e1w		H. influenzae beta-carbonic anhydrase, variant d44n in 100 mm sodium bicarbonate
3e24		H. influenzae beta-carbonic anhydrase, variant w39f
3e28		H. influenzae beta-carbonic anhydrase, variant y181f
3e2a		H. influenzae beta-carbonic anhydrase, variant y181f with mm bicarbonate
3e2w		H. influenzae beta-carbonic anhydrase, variant y181f with 1m bicarbonate
3e2x		H. influenzae beta-carbonic anhydrase, variant v47a
3e31		H. influenzae beta-carbonic anhydrase, variant v47a
3e3f		H. influenzae beta-carbonic anhydrase, variant v47a with 100 mm bicarbonate
3e3g		H. influenzae beta-carbonic anhydrase, variant g41a
3e3i		H. influenzae beta-carbonic anhydrase, variant g41a with 100 mm bicarbonate
3eyx		Crystal structure of carbonic anhydrase nce103 from saccharomyces cerevisiae

Links (links to other resources describing this domain)
PFAM Pro_CA
INTERPRO IPR001765

PFAM	Pro_CA
INTERPRO	IPR001765