Identification |
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Name: | 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase |
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Synonyms: | - 2-keto-3-deoxygluconate 5-dehydrogenase
- 2-keto-3-deoxygluconate oxidoreductase
- KDG oxidoreductase
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Gene Name: | kduD |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in 2-deoxy-D-gluconate 3-dehydrogenase activity |
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Specific Function: | Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3- deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH |
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Cellular Location: | Not Available |
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SMPDB Pathways: | - Collection of Reactions without pathways PW001891
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KEGG Pathways: | - Pentose and glucuronate interconversions ec00040
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KEGG Reactions: | |
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SMPDB Reactions: | |
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EcoCyc Reactions: | |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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2-deoxy-D-gluconate 3-dehydrogenase activity | binding | catalytic activity | NAD or NADH binding | nucleotide binding | oxidoreductase activity | oxidoreductase activity, acting on CH-OH group of donors | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | Process |
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metabolic process | oxidation reduction |
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Gene Properties |
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Blattner: | b2842 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 64.24 |
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Left Sequence End | 2980519 |
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Right Sequence End | 2981280 |
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Gene Sequence: | >762 bp
GTGATGTTGTCTGCTACTCAACCACTTAGCGAAAAATTGCCAGCGCATGGCTGCCGTCAT
GTTGCGATCATTATGGACGGCAATGGCCGCTGGGCAAAAAAGCAAGGGAAGATTCGTGCC
TTTGGGCATAAAGCCGGGGCAAAATCCGTCCGCCGGGCTGTCTCTTTTGCGGCCAACAAC
GGTATTGAGGCGTTAACGCTGTATGCCTTTAGTAGTGAAAACTGGAACCGACCAGCGCAG
GAAGTCAGTGCGTTAATGGAACTGTTTGTGTGGGCGCTCGATAGCGAAGTAAAAAGTCTG
CACCGACATAACGTGCGTCTGCGTATTATTGGCGATACCAGTCGCTTTAACTCGCGTTTG
CAAGAACGTATTCGTAAATCTGAAGCGCTAACAGCCGGGAATACCGGTCTGACGCTGAAT
ATTGCGGCGAACTACGGTGGACGTTGGGATATAGTCCAGGGAGTCAGGCAACTGGCTGAA
AAGGTGCAGCAAGGAAACCTGCAACCAGATCAGATAGATGAAGAGATGCTAAACCAGCAT
GTCTGTATGCATGAACTGGCCCCTGTAGATTTAGTAATTAGGACTGGGGGGGAGCATCGC
ATTAGTAACTTTTTGCTTTGGCAAATTGCCTATGCCGAACTTTACTTTACAGATGTTCTC
TGGCCCGATTTCGATGAACAAGACTTTGAAGGGGCGTTAAATGCCTTTGCTAATCGAGAG
CGTCGTTTCGGCGGCACCGAGCCCGGTGATGAAACAGCCTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 253 |
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Protein Molecular Weight: | 27070 |
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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: | >2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
MILSAFSLEGKVAVVTGCDTGLGQGMALGLAQAGCDIVGINIVEPTETIEQVTALGRRFL
SLTADLRKIDGIPALLDRAVAEFGHIDILVNNAGLIRREDALEFSEKDWDDVMNLNIKSV
FFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHN
INVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPIVFLASSASDYVN
GYTIAVDGGWLAR |
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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
- Condemine, G., Robert-Baudouy, J. (1991). "Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation." Mol Microbiol 5:2191-2202. Pubmed: 1766386
- 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
- Maiden, M. C., Jones-Mortimer, M. C., Henderson, P. J. (1988). "The cloning, DNA sequence, and overexpression of the gene araE coding for arabinose-proton symport in Escherichia coli K12." J Biol Chem 263:8003-8010. Pubmed: 2836407
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