Identification
Name:Carbonic anhydrase 2
Synonyms:
  • Carbonate dehydratase 2
Gene Name:can
Enzyme Class:
Biological Properties
General Function:Involved in carbonate dehydratase activity
Specific Function:H(2)CO(3) = CO(2) + H(2)O
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
carbonate dehydratase activity
catalytic activity
cation binding
hydro-lyase activity
ion binding
lyase activity
metal ion binding
transition metal ion binding
zinc ion binding
Process
carbon utilization
Gene Properties
Blattner:b0126
Gene OrientationCounterclockwise
Centisome Percentage:3.06
Left Sequence End142008
Right Sequence End142670
Gene Sequence:
>663 bp
ATGAAAGACATAGATACACTCATCAGCAACAATGCACTATGGTCAAAAATGCTGGTGGAA
GAGGATCCCGGGTTTTTTGAGAAACTGGCACAAGCGCAAAAACCGCGCTTTCTATGGATT
GGATGTTCCGACAGTCGCGTTCCTGCAGAACGTTTAACCGGTCTTGAGCCGGGCGAACTC
TTTGTTCACCGTAATGTTGCTAACCTGGTCATTCACACTGACCTGAACTGCCTTTCCGTG
GTTCAGTATGCAGTGGATGTACTCGAAGTTGAACACATTATTATCTGTGGCCACTACGGT
TGCGGCGGCGTACAAGCCGCAGTTGAAAACCCGGAACTGGGGCTTATCAACAACTGGCTG
CTGCATATCCGCGATATCTGGTTCAAACATAGCTCATTGCTCGGCGAAATGCCGCAAGAG
CGCCGTCTGGATACCTTGTGTGAACTGAACGTCATGGAACAGGTGTATAACCTGGGCCAC
TCCACCATTATGCAATCAGCGTGGAAACGCGGGCAGAAAGTTACCATTCACGGCTGGGCC
TACGGCATTCACGACGGCTTGCTGCGTGATCTGGATGTTACCGCCACCAACCGCGAAACC
CTTGAGCAACGTTACCGTCACGGGATTTCCAACCTCAAGCTGAAACACGCCAACCACAAA
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:220
Protein Molecular Weight:25097
Protein Theoretical pI:7
PDB File:1T75
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Carbonic anhydrase 2
MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGEL
FVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWL
LHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGHSTIMQSAWKRGQKVTIHGWA
YGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
References
External Links:
ResourceLink
Uniprot ID:P61517
Uniprot Name:CAN_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674342
PDB ID:1T75
Ecogene ID:EG12319
Ecocyc:EG12319
ColiBase:b0126
Kegg Gene:b0126
EchoBASE ID:EB2224
CCDB:CAN_ECOLI
BacMap:16128119
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Cronk, J. D., Endrizzi, J. A., Cronk, M. R., O'neill, J. W., Zhang, K. Y. (2001). "Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity." Protein Sci 10:911-922. Pubmed: 11316870
  • Fountoulakis, M., Takacs, M. F., Berndt, P., Langen, H., Takacs, B. (1999). "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Electrophoresis 20:2181-2195. Pubmed: 10493123
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553