Identification |
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Name: | Cytoplasmic trehalase |
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Synonyms: | - Alpha,alpha-trehalase
- Alpha,alpha-trehalose glucohydrolase
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Gene Name: | treF |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in catalytic activity |
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Specific Function: | Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity |
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Cellular Location: | Cytoplasm |
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SMPDB Pathways: | - Secondary metabolites: Trehalose Biosynthesis and Metabolism PW000968
- Starch and sucrose metabolism PW000941
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KEGG Pathways: | |
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KEGG Reactions: | |
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SMPDB Reactions: | |
1.0 | + | 1.0 | → | 1.0 | + | 1.0Beta-D-Glucose | + | 1.0 |
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EcoCyc Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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alpha,alpha-trehalase activity | catalytic activity | hydrolase activity | hydrolase activity, acting on glycosyl bonds | hydrolase activity, hydrolyzing O-glycosyl compounds | trehalase activity | Process |
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carbohydrate metabolic process | disaccharide metabolic process | metabolic process | oligosaccharide metabolic process | primary metabolic process | trehalose metabolic process |
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Gene Properties |
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Blattner: | b3519 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 79.05 |
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Left Sequence End | 3667615 |
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Right Sequence End | 3669264 |
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Gene Sequence: | >1650 bp
ATGCTCAATCAGAAAATTCAAAACCCTAATCCAGACGAACTGATGATCGAAGTCGATCTC
TGCTATGAGCTGGACCCGTATGAATTAAAACTGGATGAGATGATCGAGGCAGAACCGGAA
CCCGAGATGATTGAAGGGCTGCCTGCCTCTGATGCGCTGACGCCTGCCGATCGCTATCTC
GAACTGTTCGAGCATGTTCAGTCGGCGAAAATTTTCCCCGACAGTAAAACCTTTCCCGAC
TGCGCACCTAAAATGGACCCGCTGGATATCTTAATCCGCTACCGTAAAGTGCGCCGTCAT
CGTGATTTTGACTTGCGCAAGTTTGTTGAAAACCACTTCTGGCTGCCGGAGGTCTACTCC
AGCGAGTATGTATCGGACCCGCAAAATTCCCTGAAAGAGCATATCGACCAGCTGTGGCCG
GTGCTAACCCGCGAACCACAGGATCACATTCCGTGGTCTTCTCTGCTGGCGCTGCCGCAG
TCATATATTGTCCCGGGCGGCCGTTTTAGCGAAACCTACTATTGGGATTCCTATTTCACC
ATGCTGGGGCTGGCGGAAAGTGGTCGGGAAGATTTGCTGAAATGCATGGCCGATAACTTC
GCCTGGATGATCGAAAACTACGGTCACATCCCCAACGGCAACCGCACCTATTATTTGAGC
CGCTCGCAACCACCGGTTTTTGCGCTGATGGTGGAGTTGTTTGAAGAAGATGGTGTACGC
GGTGCGCGCCGCTATCTCGACCACCTTAAAATGGAATATGCCTTCTGGATGGACGGTGCA
GAATCGTTAATCCCTAATCAGGCCTATCGCCATGTTGTGCGGATGCCGGACGGATCGCTG
CTCAACCGTTACTGGGACGATCGCGACACGCCGCGTGACGAATCCTGGCTTGAGGACGTT
GAAACCGCGAAACATTCTGGTCGCCCGCCCAACGAGGTGTACCGCGATTTACGCGCGGGG
GCGGCCTCCGGTTGGGATTACTCTTCCCGTTGGCTGCGTGATACTGGTCGTCTGGCGAGC
ATTCGTACCACCCAGTTCATCCCCATCGATCTGAATGCCTTCCTGTTTAAACTGGAGAGC
GCCATCGCCAACATCTCGGCGCTGAAAGGCGAGAAAGAGACAGAAGCACTGTTCCGCCAG
AAAGCCAGTGCCCGTCGCGATGCGGTAAACCGTTACCTCTGGGATGATGAAAACGGCATC
TACCGCGATTACGACTGGCGACGCGAACAACTGGCGCTGTTTTCCGCTGCCGCCATTGTG
CCACTCTATGTCGGTATGGCGAACCATGAACAGGCCGATCGTCTGGCAAACGCCGTGCGC
AGTCGGTTACTGACACCTGGCGGGATTCTGGCAAGCGAGTACGAAACCGGTGAACAGTGG
GATAAACCCAACGGCTGGGCACCGTTACAATGGATGGCGATTCAGGGATTTAAAATGTAC
GGCGATGACCTTCTGGGTGATGAAATCGCGCGAAGCTGGCTGAAGACGGTGAATCAGTTC
TATCTGGAACAGCACAAACTGATCGAAAAATACCATATTGCCGATGGTGTTCCCCGCGAA
GGCGGCGGTGGCGAGTATCCGTTGCAGGATGGGTTTGGCTGGACTAACGGTGTGGTACGC
CGTTTAATTGGTTTGTACGGCGAACCATAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 549 |
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Protein Molecular Weight: | 63696 |
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Protein Theoretical pI: | 5 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Cytoplasmic trehalase
MLNQKIQNPNPDELMIEVDLCYELDPYELKLDEMIEAEPEPEMIEGLPASDALTPADRYL
ELFEHVQSAKIFPDSKTFPDCAPKMDPLDILIRYRKVRRHRDFDLRKFVENHFWLPEVYS
SEYVSDPQNSLKEHIDQLWPVLTREPQDHIPWSSLLALPQSYIVPGGRFSETYYWDSYFT
MLGLAESGREDLLKCMADNFAWMIENYGHIPNGNRTYYLSRSQPPVFALMVELFEEDGVR
GARRYLDHLKMEYAFWMDGAESLIPNQAYRHVVRMPDGSLLNRYWDDRDTPRDESWLEDV
ETAKHSGRPPNEVYRDLRAGAASGWDYSSRWLRDTGRLASIRTTQFIPIDLNAFLFKLES
AIANISALKGEKETEALFRQKASARRDAVNRYLWDDENGIYRDYDWRREQLALFSAAAIV
PLYVGMANHEQADRLANAVRSRLLTPGGILASEYETGEQWDKPNGWAPLQWMAIQGFKMY
GDDLLGDEIARSWLKTVNQFYLEQHKLIEKYHIADGVPREGGGGEYPLQDGFGWTNGVVR
RLIGLYGEP |
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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
- 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
- Horlacher, R., Uhland, K., Klein, W., Ehrmann, M., Boos, W. (1996). "Characterization of a cytoplasmic trehalase of Escherichia coli." J Bacteriol 178:6250-6257. Pubmed: 8892826
- Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620
- Uhland, K., Mondigler, M., Spiess, C., Prinz, W., Ehrmann, M. (2000). "Determinants of translocation and folding of TreF, a trehalase of Escherichia coli." J Biol Chem 275:23439-23445. Pubmed: 10816581
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