Identification |
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Name: | S-formylglutathione hydrolase frmB |
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Synonyms: | |
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Gene Name: | frmB |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in carboxylesterase activity |
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Specific Function: | Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against two pNP-esters (pNP- acetate and pNP-propionate), alpha-naphthyl acetate and lactoylglutathione |
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Cellular Location: | Cytoplasmic |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | - Methane metabolism ec00680
- Microbial metabolism in diverse environments ec01120
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KEGG Reactions: | |
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EcoCyc Reactions: | |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Component |
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cytoplasmic membrane-bounded vesicle | cytoplasmic vesicle | organelle | vesicle | Function |
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carboxylesterase activity | catalytic activity | hydrolase activity | hydrolase activity, acting on ester bonds | S-formylglutathione hydrolase activity | thiolester hydrolase activity |
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Gene Properties |
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Blattner: | b0355 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 8.12 |
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Left Sequence End | 376759 |
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Right Sequence End | 377592 |
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Gene Sequence: | >834 bp
ATGGAACTCATTGAAAAACATGTCAGCTTTGGCGGCTGGCAAAATATGTATCGGCATTAT
TCCCAATCACTGAAATGTGAAATGAATGTCGGCGTCTATCTCCCACCAAAAGCCGCGAAT
GAAAAATTGCCGGTGCTGTACTGGCTTTCAGGCCTGACCTGCAACGAGCAGAATTTCATT
ACTAAATCGGGGATGCAGCGTTACGCGGCTGAGCACAACATTATTGTTGTTGCGCCGGAC
ACCAGTCCGCGAGGCAGTCATGTCGCAGATGCTGACCGTTACGATCTCGGGCAAGGTGCC
GGGTTTTACCTGAACGCGACGCAAGCGCCGTGGAATGAACATTACAAAATGTATGACTAT
ATCCGCAACGAGCTGCCGGATTTAGTGATGCATCATTTTCCGGCAACGGCCAAAAAGTCT
ATCTCTGGTCATTCTATGGGCGGGCTGGGCGCGCTGGTGCTGGCGTTACGTAACCCAGAT
GAATATGTCAGCGTCTCGGCGTTTTCGCCCATTGTCTCCCCATCGCAAGTGCCGTGGGGA
CAGCAAGCCTTTGCTGCATATCTTGCTGAAAATAAAGATGCCTGGTTGGATTACGACCCG
GTGAGTCTTATTTCACAAGGTCAACGCGTTGCGGAAATCATGGTTGATCAGGGGTTGAGT
GATGATTTTTACGCAGAACAGCTGCGGACTCCAAATCTTGAAAAGATCTGCCAGGAGATG
AATATCAAGACGTTAATCCGTTATCACGAGGGTTATGATCACAGCTATTATTTTGTCTCC
AGTTTTATTGGCGAGCATATTGCCTACCACGCCAATAAACTGAATATGCGTTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 277 |
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Protein Molecular Weight: | 31424 |
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Protein Theoretical pI: | 6 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >S-formylglutathione hydrolase frmB
MELIEKHVSFGGWQNMYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFI
TKSGMQRYAAEHNIIVVAPDTSPRGSHVADADRYDLGQGAGFYLNATQAPWNEHYKMYDY
IRNELPDLVMHHFPATAKKSISGHSMGGLGALVLALRNPDEYVSVSAFSPIVSPSQVPWG
QQAFAAYLAENKDAWLDYDPVSLISQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQEM
NIKTLIRYHEGYDHSYYFVSSFIGEHIAYHANKLNMR |
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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
- Gonzalez, C. F., Proudfoot, M., Brown, G., Korniyenko, Y., Mori, H., Savchenko, A. V., Yakunin, A. F. (2006). "Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG." J Biol Chem 281:14514-14522. Pubmed: 16567800
- 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
- Herring, C. D., Blattner, F. R. (2004). "Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR." J Bacteriol 186:6714-6720. Pubmed: 15466022
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