Identification |
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Name: | 2,5-diketo-D-gluconic acid reductase A |
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Synonyms: | - 2,5-DKG reductase A
- 2,5-DKGR A
- 25DKGR-A
- AKR5C
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Gene Name: | dkgA |
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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 reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives |
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Cellular Location: | Cytoplasm |
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SMPDB Pathways: | |
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KEGG Pathways: | Not Available |
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KEGG Reactions: | |
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SMPDB Reactions: | |
1.0 | + | 1.0 | + | 1.0NADPH | + | 1.0 | → | 1.0 | + | 1.02-Keto-L-gluconate | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0Hydroxyacetone | + | 1.0 |
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EcoCyc Reactions: | |
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Complex Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 2.0-Dehydro-L-gulonate | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | → | 1.0Acetol | + | 1.0 |
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Metabolites: | |
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GO Classification: | Function |
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catalytic activity | oxidoreductase activity | Process |
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metabolic process | oxidation reduction |
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Gene Properties |
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Blattner: | b3012 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 67.99 |
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Left Sequence End | 3154645 |
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Right Sequence End | 3155472 |
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Gene Sequence: | >828 bp
ATGAGTGTGCTCATTAATGAAAAACTGCATTCGCGGCGGCTGAAATGGCGCTGGCCGCTC
TCGCGTCAGGTGACCTTAAGCATTGGCACGTTAGCGGTTTTACTCACCGTATGGTGGACG
GTGGCGACGCTGCAACTGATTAGCCCGCTATTTTTGCCGCCGCCGCAACAGGTACTGGAA
AAACTACTCACCATTGCCGGACCGCAAGGCTTTATGGACGCCACGCTGTGGCAGCATCTG
GCAGCCAGTCTGACGCGCATTATGCTGGCGCTATTTGCAGCGGTGTTGTTCGGTATTCCG
GTCGGGATCGCGATGGGACTTAGCCCTACGGTACGCGGCATTCTGGATCCGATAATCGAG
CTTTATCGTCCGGTGCCGCCGCTGGCTTATTTGCCGCTGATGGTGATCTGGTTTGGTATT
GGTGAAACCTCGAAGATCTTACTGATCTATTTAGCGATTTTTGCACCGGTGGCGATGTCG
GCGCTGGCGGGGGTGAAAAGCGTGCAGCAGGTTCGCATTCGTGCCGCCCAGTCGCTGGGT
GCCAGCCGTGCGCAGGTGCTGTGGTTTGTCATTTTGCCCGGTGCGCTGCCGGAAATCCTC
ACCGGATTACGTATTGGTCTGGGGGTGGGCTGGTCTACGCTGGTGGCGGCGGAGCTGATT
GCCGCGACGCGCGGTTTAGGATTTATGGTTCAGTCAGCGGGTGAATTTCTCGCAACTGAC
GTGGTGCTGGCGGGGATCGCGGTGATTGCGATTATCGCCTTTCTTTTAGAACTGGGTCTG
CGCGCGTTACAGCGCCGCCTGACGCCCTGGCATGGAGAAGTACAATGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 275 |
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Protein Molecular Weight: | 31109 |
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Protein Theoretical pI: | 6 |
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PDB File: | 1MZR |
Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >2,5-diketo-D-gluconic acid reductase A
MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIQKALEVGYRSIDTAAAYKNEEGVGKA
LKNASVNREELFITTKLWNDDHKRPREALLDSLKKLQLDYIDLYLMHWPVPAIDHYVEAW
KGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHK
IQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAE
NFDVWDFRLDKDELGEIAKLDQGKRLGPDPDQFGG |
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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
- Habrych, M., Rodriguez, S., Stewart, J. D. (2002). "Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE." Biotechnol Prog 18:257-261. Pubmed: 11934293
- 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
- Jeudy, S., Monchois, V., Maza, C., Claverie, J. M., Abergel, C. (2006). "Crystal structure of Escherichia coli DkgA, a broad-specificity aldo-keto reductase." Proteins 62:302-307. Pubmed: 16284956
- Yum, D. Y., Lee, B. Y., Pan, J. G. (1999). "Identification of the yqhE and yafB genes encoding two 2, 5-diketo-D-gluconate reductases in Escherichia coli." Appl Environ Microbiol 65:3341-3346. Pubmed: 10427017
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