Identification |
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Name: | Carbonic anhydrase 1 |
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Synonyms: | |
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Gene Name: | cynT |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in carbonate dehydratase activity |
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Specific Function: | Reversible hydration of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (cynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate |
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Cellular Location: | Not Available |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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KEGG Reactions: | |
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SMPDB Reactions: | |
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EcoCyc Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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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 |
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carbon utilization |
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Gene Properties |
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Blattner: | b0339 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 7.72 |
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Left Sequence End | 358023 |
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Right Sequence End | 358682 |
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Gene Sequence: | >660 bp
GTGAAAGAGATTATTGATGGATTCCTTAAATTCCAGCGCGAGGCATTTCCGAAGCGGGAA
GCCTTGTTTAAACAGCTGGCGACACAGCAAAGCCCGCGCACACTTTTTATCTCCTGCTCC
GACAGCCGTCTGGTCCCTGAGCTGGTGACGCAACGTGAGCCTGGCGATCTGTTCGTTATT
CGCAACGCGGGCAATATCGTCCCTTCCTACGGGCCGGAACCCGGTGGCGTTTCTGCTTCG
GTGGAGTATGCCGTCGCTGCGCTTCGGGTATCTGACATTGTGATTTGTGGTCATTCCAAC
TGTGGCGCGATGACCGCCATTGCCAGCTGTCAGTGCATGGACCATATGCCTGCCGTCTCC
CACTGGCTGCGTTATGCCGATTCAGCCCGCGTCGTTAATGAGGCGCGCCCGCATTCCGAT
TTACCGTCAAAAGCTGCGGCGATGGTACGTGAAAACGTCATTGCTCAGTTGGCTAATTTG
CAAACTCATCCATCGGTGCGCCTGGCGCTCGAAGAGGGGCGGATCGCCCTGCACGGCTGG
GTCTACGACATTGAAAGCGGCAGCATCGCAGCTTTTGACGGCGCAACCCGCCAGTTTGTG
CCACTGGCCGCTAATCCTCGCGTTTGTGCCATACCGCTACGCCAACCGACCGCAGCGTAA
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 219 |
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Protein Molecular Weight: | 23764 |
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Protein Theoretical pI: | 7 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Carbonic anhydrase 1
MKEIIDGFLKFQREAFPKREALFKQLATQQSPRTLFISCSDSRLVPELVTQREPGDLFVI
RNAGNIVPSYGPEPGGVSASVEYAVAALRVSDIVICGHSNCGAMTAIASCQCMDHMPAVS
HWLRYADSARVVNEARPHSDLPSKAAAMVRENVIAQLANLQTHPSVRLALEEGRIALHGW
VYDIESGSIAAFDGATRQFVPLAANPRVCAIPLRQPTAA |
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References |
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External Links: | |
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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
- Guilloton, M. B., Korte, J. J., Lamblin, A. F., Fuchs, J. A., Anderson, P. M. (1992). "Carbonic anhydrase in Escherichia coli. A product of the cyn operon." J Biol Chem 267:3731-3734. Pubmed: 1740425
- 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
- Sung, Y. C., Fuchs, J. A. (1988). "Characterization of the cyn operon in Escherichia coli K12." J Biol Chem 263:14769-14775. Pubmed: 3049588
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