| Identification |
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| Name: | Gluconate 5-dehydrogenase |
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| Synonyms: | - 5-keto-D-gluconate 5-reductase
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| Gene Name: | idnO |
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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 a reversible reduction of 5-ketoglutanate to form D-gluconate. Dependent on NADP, almost inactive with NAD |
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| Cellular Location: | Cytoplasm (Probable) |
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| SMPDB Pathways: | |
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| KEGG Pathways: | Not Available |
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| KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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| SMPDB Reactions: | |
1.05-Keto-D-gluconate | + | 1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
1.0NAD(P)+ | + | 1.0 | ↔ | 1.0NAD(P)H | + | 1.0 | + | 1.0 |
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| Complex Reactions: | | | |
1.0 | + | 1.0NAD(P)(+) | → | 1.0 | + | 1.0NAD(P)H |
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| Metabolites: | |
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| GO Classification: | | Function |
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| binding | | catalytic activity | | oxidoreductase activity | | Process |
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| metabolic process | | oxidation reduction |
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| Gene Properties |
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| Blattner: | b4266 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 96.79 |
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| Left Sequence End | 4490610 |
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| Right Sequence End | 4491374 |
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| Gene Sequence: | >765 bp
ATGCAAGCATTGCTGGAACACTTTATTACCCAATCCACCGTGTATTCATTGATGGCGGTG
GTGTTGGTGGCCTTTCTGGAGTCGCTGGCGCTGGTCGGTTTGATTCTACCCGGTACGGTG
CTGATGGCGGGGCTGGGAGCGCTGATTGGCAGCGGCGAGTTAAGTTTCTGGCACGCCTGG
CTGGCAGGGATTATTGGCTGCTTGATGGGCGACTGGATTTCTTTCTGGCTGGGTTGGCGT
TTTAAAAAGCCGTTGCATCGCTGGTCATTTCTGAAGAAAAACAAAGCACTACTTGATAAA
ACTGAACATGCGTTGCATCAACACAGCATGTTCACCATTCTGGTCGGTCGTTTTGTTGGC
CCGACGCGTCCGCTGGTGCCAATGGTGGCGGGAATGCTGGATCTGCCGGTGGCTAAATTT
ATTACGCCGAATATTATCGGCTGCCTGCTGTGGCCGCCGTTTTACTTCCTGCCAGGGATT
CTGGCGGGCGCGGCGATCGATATTCCTGCCGGAATGCAGAGCGGTGAGTTTAAATGGTTG
CTGCTGGCAACAGCGGTGTTTTTGTGGGTTGGTGGCTGGCTGTGCTGGCGGTTATGGCGC
AGCGGTAAAGCGACTGACCGTTTGAGTCATTATTTGTCCCGCGGTCGTTTGTTGTGGCTG
ACGCCGTTGATTTCTGCCATCGGCGTGGTGGCGCTGGTGGTGTTAATTCGCCACCCGTTG
ATGCCGGTGTATATCGATATTTTGCGTAAAGTGGTTGGGGTTTAG |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 254 |
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| Protein Molecular Weight: | 27563 |
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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: | >Gluconate 5-dehydrogenase
MNDLFSLAGKNILITGSAQGIGFLLATGLGKYGAQIIINDITAERAELAVEKLHQEGIQA
VAAPFNVTHKHEIDAAVEHIEKDIGPIDVLVNNAGIQRRHPFTEFPEQEWNDVIAVNQTA
VFLVSQAVTRHMVERKAGKVINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHN
IQVNGIAPGYFKTEMTKALVEDEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVN
GHLLFVDGGMLVAV |
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| References |
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| External Links: | |
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| General Reference: | - Bausch, C., Peekhaus, N., Utz, C., Blais, T., Murray, E., Lowary, T., Conway, T. (1998). "Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli." J Bacteriol 180:3704-3710. Pubmed: 9658018
- 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
- Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
- 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
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