| Identification |
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| Name: | Glyoxylate/hydroxypyruvate reductase B |
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| Synonyms: | - 2-ketoaldonate reductase
- 2-ketogluconate reductase
- 2KR
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| Gene Name: | ghrB |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
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| Specific Function: | Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D- gluconate (5KDG), 2-keto-D-gluconate (2KDG) to D-gluconate, and 2- keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D-fructose and L- sorbose. Activity with NAD is very low |
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| Cellular Location: | Cytoplasm (Probable) |
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| SMPDB Pathways: | |
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| KEGG Pathways: | - Glyoxylate and dicarboxylate metabolism ec00630
- Metabolic pathways eco01100
- Microbial metabolism in diverse environments ec01120
- Pentose phosphate pathway ec00030
- Pyruvate metabolism ec00620
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| KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | ↔ | 1.02-Keto-D-gluconic acid | + | 1.0 | + | 1.0 | + | 1.0 |
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| SMPDB Reactions: | |
1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.05-Keto-D-gluconate | + | 1.0 |
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1.02-Keto-L-gluconate | + | 1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 |
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| Complex Reactions: | | | |
2.0-Dehydro-L-gulonate | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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2.0-Dehydro-L-gulonate | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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2.0-Dehydro-L-gulonate | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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2.0-Dehydro-L-gulonate | + | 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 | | cofactor binding | | 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 |
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| Gene Properties |
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| Blattner: | b3553 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 80.08 |
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| Left Sequence End | 3715333 |
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| Right Sequence End | 3716307 |
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| Gene Sequence: | >975 bp
ATGAAATTACAACAACTTCGCTATATTGTTGAGGTGGTCAATCATAACCTGAATGTCTCA
TCAACAGCGGAAGGACTTTACACATCACAACCCGGGATCAGTAAACAAGTCAGAATGCTG
GAAGACGAGCTAGGCATTCAAATTTTTTCCCGAAGCGGCAAGCACCTGACGCAGGTAACG
CCAGCAGGGCAAGAAATAATTCGTATCGCTCGCGAAGTCCTGTCGAAAGTCGATGCCATA
AAATCGGTTGCCGGAGAGCACACCTGGCCGGATAAAGGTTCACTGTATATCGCCACCACG
CATACCCAGGCACGCTACGCATTACCAAACGTCATCAAAGGCTTTATTGAGCGTTATCCT
CGCGTTTCTTTGCATATGCACCAGGGCTCGCCGACACAAATTGCTGATGCCGTCTCTAAA
GGCAATGCTGATTTCGCTATCGCCACAGAAGCGCTGCATCTGTATGAAGATTTAGTGATG
TTACCGTGCTACCACTGGAATCGGGCTATTGTAGTCACTCCGGATCACCCGCTGGCAGGC
AAAAAAGCCATTACCATTGAAGAACTGGCGCAATATCCGTTGGTGACATATACCTTCGGC
TTTACCGGACGTTCAGAACTGGATACTGCCTTTAATCGCGCAGGGTTAACGCCGCGTATC
GTTTTCACGGCAACGGATGCTGACGTCATTAAAACTTACGTCCGGTTAGGGCTGGGGGTA
GGGGTCATTGCCAGCATGGCGGTGGATCCGGTCGCCGATCCCGACCTTGTGCGTGTTGAT
GCTCACGATATCTTCAGCCACAGTACAACCAAAATTGGTTTTCGCCGTAGTACTTTCTTG
CGCAGTTATATGTATGATTTCATTCAGCGTTTTGCACCGCATTTAACGCGTGATGTCGTT
GATGCGGCTGTCGCATTGCGCTCTAATGAAGAAATTGAGGTCATGTTTAAAGATATAAAA
CTGCCGGAAAAATAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 324 |
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| Protein Molecular Weight: | 35395 |
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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: | >Glyoxylate/hydroxypyruvate reductase B
MKPSVILYKALPDDLLQRLQEHFTVHQVANLSPQTVEQNAAIFAEAEGLLGSNENVNAAL
LEKMPKLRATSTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVE
VAERVKAGEWTASIGPDWYGTDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHH
KEAEERFNARYCDLDTLLQESDFVCLILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPV
VDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSMANVVAVPHIGSATHETRYGMAAC
AVDNLIDALQGKVEKNCVNPHVAD |
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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
- Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
- Nunez, M. F., Pellicer, M. T., Badia, J., Aguilar, J., Baldoma, L. (2001). "Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli." Biochem J 354:707-715. Pubmed: 11237876
- 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
- Yum, D. Y., Lee, B. Y., Hahm, D. H., Pan, J. G. (1998). "The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase." J Bacteriol 180:5984-5988. Pubmed: 9811658
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