Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015

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 [Smith00a]. 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: [Smith00a, 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

Smith00a: 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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Mon Aug 31, 2015, BIOCYC14B.