| Identification |
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| Name: | Glycerol dehydrogenase |
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| Synonyms: | |
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| Gene Name: | gldA |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in oxidoreductase activity |
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| Specific Function: | Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of gldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively |
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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: | |
1.0 | + | 1.0 | + | 1.0 | ← | 1.0 | + | 1.0 | + | 1.0 |
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1.0Hydroxyacetone | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | |
1.0Acetol | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Function |
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| binding | | catalytic activity | | cation binding | | ion binding | | metal ion binding | | oxidoreductase activity | | oxidoreductase activity, acting on CH-OH group of donors | | Process |
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| metabolic process | | oxidation reduction |
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| Gene Properties |
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| Blattner: | b3945 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 89.14 |
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| Left Sequence End | 4135955 |
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| Right Sequence End | 4137058 |
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| Gene Sequence: | >1104 bp
ATGAGTGACAGCCAGACGCTGGTGGTAAAACTCGGCACCAGTGTGCTAACAGGCGGATCG
CGCCGTCTGAACCGTGCCCATATCGTTGAACTTGTTCGCCAGTGCGCGCAGTTACATGCC
GCCGGGCATCGGATTGTTATTGTGACGTCGGGCGCGATCGCCGCCGGACGTGAGCACCTG
GGTTACCCGGAACTGCCAGCGACCATCGCCTCGAAACAACTGCTGGCGGCGGTAGGGCAG
AGTCGACTGATTCAACTGTGGGAACAGCTGTTTTCGATTTATGGCATTCACGTCGGGCAA
ATGCTGCTGACCCGTGCTGATATGGAAGACCGTGAACGCTTCCTGAACGCCCGCGACACC
CTGCGAGCGTTGCTCGATAACAATATCGTTCCGGTAATCAATGAGAACGATGCTGTCGCT
ACGGCAGAGATTAAGGTCGGCGATAACGATAACCTTTCTGCGCTGGCGGCGATTCTTGCG
GGTGCCGATAAACTGTTGCTGCTGACCGATCAAAAAGGTTTGTATACCGCTGACCCGCGC
AGCAATCCGCAGGCAGAACTGATTAAAGATGTTTACGGCATTGATGACGCACTGCGCGCG
ATTGCCGGTGACAGCGTTTCAGGCCTCGGAACTGGCGGCATGAGTACCAAATTGCAGGCC
GCTGACGTGGCTTGCCGTGCGGGTATCGACACCATTATTGCCGCGGGCAGCAAGCCGGGC
GTTATTGGTGATGTGATGGAAGGCATTTCCGTCGGTACGCTGTTCCATGCCCAGGCGACT
CCGCTTGAAAACCGTAAACGCTGGATTTTCGGTGCGCCGCCGGCGGGTGAAATCACGGTA
GATGAAGGGGCAACTGCCGCCATTCTGGAACGCGGCAGCTCCCTGTTGCCGAAAGGCATT
AAAAGCGTGACTGGCAATTTCTCGCGTGGTGAAGTCATCCGCATTTGCAACCTCGAAGGC
CGCGATATCGCCCACGGCGTCAGTCGTTACAACAGCGATGCATTACGCCGTATTGCCGGA
CACCACTCGCAAGAAATTGATGCAATACTGGGATATGAATACGGCCCGGTTGCCGTTCAC
CGTGATGACATGATTACCCGTTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 367 |
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| Protein Molecular Weight: | 38712 |
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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: | >Glycerol dehydrogenase
MDRIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVE
IAPFGGECSQNEIDRLRGIAETAQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIAST
DAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAAGIGDALATWFEAR
ACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYL
SGVGFESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALS
HAVGLPITLAQLDIKEDVPAKMRIVAEAACAEGETIHNMPGGATPDQVYAALLVADQYGQ
RFLQEWE |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
- 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, R., Murarka, A., Dharmadi, Y., Yazdani, S. S. (2008). "A new model for the anaerobic fermentation of glycerol in enteric bacteria: trunk and auxiliary pathways in Escherichia coli." Metab Eng 10:234-245. Pubmed: 18632294
- 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
- Subedi, K. P., Kim, I., Kim, J., Min, B., Park, C. (2008). "Role of GldA in dihydroxyacetone and methylglyoxal metabolism of Escherichia coli K12." FEMS Microbiol Lett 279:180-187. Pubmed: 18179582
- Tang, C. T., Ruch, F. E. Jr, Lin, C. C. (1979). "Purification and properties of a nicotinamide adenine dinucleotide-linked dehydrogenase that serves an Escherichia coli mutant for glycerol catabolism." J Bacteriol 140:182-187. Pubmed: 40950
- Truniger, V., Boos, W. (1994). "Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase." J Bacteriol 176:1796-1800. Pubmed: 8132480
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