Escherichia coli K-12 substr. MG1655 Enzyme: carbonic anhydrase 2

Gene: can Accession Numbers: EG12319 (EcoCyc), b0126, ECK0125

Synonyms: yadF

Regulation Summary Diagram: ?

Regulation summary diagram for can

Subunit composition of carbonic anhydrase 2 = [Can]4
         carbonic anhydrase 2 monomer = Can

E. coli encodes two carbonic anhydrases, Can (carbonic anhydrase 2) and CynT (carbonic anhydrase 1). Can belongs to Clade B of the β class of carbonic anhydrases [Smith00]. Carbonic anhydrase 2 is essential for growth at amospheric pCO2 [Hashimoto03, Merlin03, Baba06]. Enzymatic activity of carbonic anhydrase 2 is pH-dependent [Cronk01].

Crystal structures of carbonic anhydrase 2 have been solved. The crystal structure data as well as size exclusion chromatography indicate that the protein exists as a homotetramer in solution [Cronk01]. There is structural evidence for a noncatalytic binding site for bicarbonate [Cronk06].

A can mutant does not grow under normal atmospheric conditions, but the mutant can grow under conditions with a high exogenous or endogenous supply of CO2. Expression of cynT suppresses phenotypes of a can mutant [Merlin03]. A can cynT double mutant is only viable under high CO2 conditions [Hashimoto03].

Expression of can is inversely proportional to the growth rate and does not depend on CO2 levels [Merlin03]. Under anaerobiosis, FNR represses can gene expression, but it is not known if this regulation is direct or indirect [Salmon03].

Can: "carbonic anhydrase" [Merlin03]

Reviews: [Smith00, Kozliak00, Tripp01]

Citations: [BolanosGarcia06]

Gene Citations: [Nonaka06]

Locations: cytosol

Map Position: [142,008 <- 142,670] (3.06 centisomes, 11°)
Length: 663 bp / 220 aa

Molecular Weight of Polypeptide: 25.097 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000442 , DIP:DIP-36168N , EchoBASE:EB2224 , EcoGene:EG12319 , EcoliWiki:b0126 , ModBase:P61517 , OU-Microarray:b0126 , PortEco:can , Pride:P61517 , Protein Model Portal:P61517 , RefSeq:NP_414668 , RegulonDB:EG12319 , SMR:P61517 , String:511145.b0126 , UniProt:P61517

Relationship Links: InterPro:IN-FAMILY:IPR001765 , InterPro:IN-FAMILY:IPR015892 , Panther:IN-FAMILY:PTHR11002 , PDB:Structure:1I6O , PDB:Structure:1I6P , PDB:Structure:1T75 , PDB:Structure:2ESF , Pfam:IN-FAMILY:PF00484 , Prosite:IN-FAMILY:PS00704 , Prosite:IN-FAMILY:PS00705 , Smart:IN-FAMILY:SM00947

In Paralogous Gene Group: 42 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred from experiment Author statement Inferred by computational analysis [UniProtGOA11a, GOA01, GOA01a, Hashimoto03, Cronk01]
GO:0015976 - carbon utilization Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004089 - carbonate dehydratase activity Inferred from experiment Author statement Inferred by computational analysis [GOA01, GOA01a, Hashimoto03, Cronk01]
GO:0008270 - zinc ion binding Inferred from experiment Inferred by computational analysis [GOA01a, Cronk01, Sevcenco11]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Lasserre06]

MultiFun Terms: metabolism central intermediary metabolism unassigned reversible reactions

Essentiality data for can knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Created 29-Mar-2007 by Keseler I , SRI International
Last-Curated ? 16-Apr-2012 by Keseler I , SRI International

Enzymatic reaction of: carbonic anhydrase

Synonyms: carbonate dehydratase, anhydrase, carbonate anhydrase, carbonic acid anhydrase, carboxyanhydrase, carbonate hydro-lyase

EC Number:

hydrogen carbonate + H+ <=> CO2 + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Cofactors or Prosthetic Groups: Zn2+ [Cronk01]

Sequence Features

Protein sequence of carbonic anhydrase 2 monomer with features indicated

Feature Class Location Citations Comment
Metal-Binding-Site 42
UniProt: Zinc.
Metal-Binding-Site 44
UniProt: Zinc.
Metal-Binding-Site 98
UniProt: Zinc.
Metal-Binding-Site 101
UniProt: Zinc.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b0126 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12319; confirmed by SwissProt match.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

BolanosGarcia06: Bolanos-Garcia VM, Davies OR (2006). "Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography." Biochim Biophys Acta 1760(9);1304-13. PMID: 16814929

Cronk01: Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY (2001). "Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity." Protein Sci 10(5);911-22. PMID: 11316870

Cronk06: Cronk JD, Rowlett RS, Zhang KY, Tu C, Endrizzi JA, Lee J, Gareiss PC, Preiss JR (2006). "Identification of a novel noncatalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase." Biochemistry 45(14);4351-61. PMID: 16584170

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hashimoto03: Hashimoto M, Kato J (2003). "Indispensability of the Escherichia coli carbonic anhydrases YadF and CynT in cell proliferation at a low CO2 partial pressure." Biosci Biotechnol Biochem 67(4);919-22. PMID: 12784642

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kozliak00: Kozliak EI, Guilloton MB, Fuchs JA, Anderson PM (2000). "Bacterial carbonic anhydrases." EXS (90);547-65. PMID: 11268536

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Merlin03: Merlin C, Masters M, McAteer S, Coulson A (2003). "Why is carbonic anhydrase essential to Escherichia coli?." J Bacteriol 185(21);6415-24. PMID: 14563877

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Sevcenco11: Sevcenco AM, Pinkse MW, Wolterbeek HT, Verhaert PD, Hagen WR, Hagedoorn PL (2011). "Exploring the microbial metalloproteome using MIRAGE." Metallomics 3(12);1324-30. PMID: 22094925

Smith00: Smith KS, Ferry JG (2000). "Prokaryotic carbonic anhydrases." FEMS Microbiol Rev 24(4);335-66. PMID: 10978542

Tripp01: Tripp BC, Smith K, Ferry JG (2001). "Carbonic anhydrase: new insights for an ancient enzyme." J Biol Chem 276(52);48615-8. PMID: 11696553

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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