| Identification |
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| Name: | Quinone oxidoreductase 1 |
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| Synonyms: | - NADPH:quinone reductase 1
- Zeta-crystallin homolog protein
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| Gene Name: | qorA |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in zinc ion binding |
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| Specific Function: | NADPH + 2 quinone = NADP(+) + 2 semiquinone |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | Not Available |
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| KEGG Pathways: | Not Available |
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| KEGG Reactions: | |
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| Complex Reactions: | |
1.0 | + | 2.0 | → | 1.0 | + | 2.0semiquinone |
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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 | | transition metal ion binding | | zinc ion binding | | Process |
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| metabolic process | | oxidation reduction |
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| Gene Properties |
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| Blattner: | b4051 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 91.84 |
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| Left Sequence End | 4261271 |
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| Right Sequence End | 4262254 |
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| Gene Sequence: | >984 bp
GTGGAAGCGATTAAGGGATCGGACGTTAATGTCCCGGATGCAGTATTTGCCTGGATGCTG
GATGGTAGAGGCGGCGTTAAACCGCTGGAAAATACAGATGTGATTGATGAAGCGCATCCC
TGTTGGCTCCACCTTAATTATGTACACCATGATAGCGCCCAATGGCTGGCGACAACACCG
CTGCTTCCCAATAACGTACGTGATGCGCTGGCGGGCGAGAGCACGCGTCCCCGAGTCAGC
CGTCTCGGTGAAGGCACGCTGATTACATTGCGCTGTATAAACGGCAGCACCGATGAACGC
CCCGATCAACTGGTCGCCATGCGTGTATATATGGACGGGCGGTTAATTGTTTCGACCCGA
CAACGCAAAGTGCTGGCGCTGGACGATGTGGTGAGCGATCTGGAAGAGGGCACGGGTCCG
ACCGATTGCGGGGGATGGCTGGTGGATGTGTGCGATGCGTTGACCGATCATTCCAGTGAA
TTTATCGAGCAGCTGCACGATAAAATTATCGACCTTGAAGATAATCTCCTTGATCAGCAA
ATTCCACCGCGTGGATTCCTGGCTCTGCTGCGCAAACAATTAATTGTGATGCGTCGCTAT
ATGGCACCGCAACGTGATGTTTATGCTCGTCTTGCCAGTGAACGTTTGCCGTGGATGAGC
GATGACCAACGCCGTCGGATGCAGGATATTGCCGATCGCCTTGGGCGCGGCCTTGACGAA
ATCGACGCCTGTATAGCACGGACTGGCGTGATGGCGGATGAAATCGCTCAGGTGATGCAG
GAAAATTTAGCTCGTCGTACCTATACAATGTCGTTGATGGCAATGGTCTTTTTACCCAGT
ACCTTTCTGACCGGGTTATTTGGCGTCAACCTTGGTGGGATCCCTGGCGGCGGGTGGCAA
TTCGGATTTTCAATTTTTTGTATTCTGTTAGTTGTTCTTATTGGTGGTGTTGCTTTATGG
TTGCATCGTAGTAAATGGTTGTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 327 |
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| Protein Molecular Weight: | 35172 |
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| Protein Theoretical pI: | 9 |
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| PDB File: | 1QOR |
| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Quinone oxidoreductase 1
MATRIEFHKHGGPEVLQAVEFTPADPAENEIQVENKAIGINFIDTYIRSGLYPPPSLPSG
LGTEAAGIVSKVGSGVKHIKAGDRVVYAQSALGAYSSVHNIIADKAAILPAAISFEQAAA
SFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGTAQKAQS
ALKAGAWQVINYREEDLVERLKEITGGKKVRVVYDSVGRDTWERSLDCLQRRGLMVSFGN
SSGAVTGVNLGILNQKGSLYVTRPSLQGYITTREELTEASNELFSLIASGVIKVDVAEQQ
KYPLKDAQRAHEILESRATQGSSLLIP |
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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
- 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
- Thorn, J. M., Barton, J. D., Dixon, N. E., Ollis, D. L., Edwards, K. J. (1995). "Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH." J Mol Biol 249:785-799. Pubmed: 7602590
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