Identification |
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Name: | NADPH-dependent 7-cyano-7-deazaguanine reductase |
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Synonyms: | - 7-cyano-7-carbaguanine reductase
- NADPH-dependent nitrile oxidoreductase
- PreQ(0) reductase
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Gene Name: | queF |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
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Specific Function: | Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) |
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Cellular Location: | Cytoplasm (Probable) |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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KEGG Reactions: | |
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SMPDB Reactions: | |
1.0 | + | 3.0 | + | 2.0NADPH | + | 2.0 | → | 2.0 | + | 1.0 |
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1.0 | + | 3.0 | + | 2.0NADPH | + | 2.0 | → | 1.0Queuine | + | 2.0 | + | 1.0 |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Component |
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cell part | cytoplasm | intracellular part | Function |
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catalytic activity | oxidoreductase activity | oxidoreductase activity, acting on other nitrogenous compounds as donors | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor | Process |
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cellular macromolecule metabolic process | macromolecule metabolic process | metabolic process | ncRNA metabolic process | oxidation reduction | queuosine biosynthetic process | RNA metabolic process | tRNA metabolic process | tRNA modification | tRNA processing |
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Gene Properties |
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Blattner: | b2794 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 63.01 |
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Left Sequence End | 2923370 |
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Right Sequence End | 2924218 |
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Gene Sequence: | >849 bp
ATGAGAAACAAACTCTCTTTCGACTTGCAGTTGAGCGCCAGAAAAGCGGCAATCGCTGAA
CGGATTGCCGCCCATAAAATTGCCCGCAGTAAAGTGTCGGTCTTTTTAATGGCGATGTCC
GCTGGCGTGTTTATGGCGATCGGATTTACTTTTTACCTTTCCGTTATCGCCGATGCCCCG
TCTTCACAGGCATTAACCCATCTGGTGGGCGGCCTTTGCTTTACACTCGGCTTTATTTTG
CTGGCGGTTTGCGGCACCAGCCTGTTCACCTCGTCGGTAATGACGGTGATGGCAAAAAGT
CGGGGCGTTATTAGTTGGCGAACTTGGCTGATTAACGCACTTCTGGTGGCCTGCGGTAAT
CTGGCAGGTATTGCCTGTTTCAGTTTGTTAATCTGGTTTTCCGGGCTGGTGATGAGTGAA
AACGCGATGTGGGGAGTCGCGGTTTTACACTGCGCCGAGGGCAAAATGCATCATACATTT
ACTGAATCTGTCAGCCTCGGCATTATGTGCAATCTGATGGTTTGCCTGGCGCTGTGGATG
AGTTATTGCGGGCGTTCGTTATGCGACAAAATCGTCGCCATGATTTTGCCCATCACCCTG
TTTGTCGCCAGTGGCTTTGAGCACTGTATCGCCAATTTGTTTGTGATTCCGTTCGCCATT
GCCATTCGCCATTTCGCCCCTCCCCCCTTCTGGCAGCTGGCGCACAGTAGCGCAGACAAT
TTTCCGGCACTGACGGTCAGCCATTTTATTACCGCCAATCTGCTCCCGGTGATGCTGGGT
AATATTATCGGCGGTGCGGTGCTGGTGAGTATGTGTTATCGGGCTATTTATTTACGTCAG
GAACCCTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 282 |
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Protein Molecular Weight: | 32587 |
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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: | >NADPH-dependent 7-cyano-7-deazaguanine reductase
MSSYANHQALAGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLKADNLPFHGTDIWTLY
ELSWLNAKGLPQVAVGHVELDYTSVNLIESKSFKLYLNSFNQTRFNNWDEVRQTLERDLS
TCAQGKISVALYRLDELEGQPIGHFNGTCIDDQDITIDNYEFTTDYLENATCGEKVVEET
LVSHLLKSNCLITHQPDWGSLQIQYRGRQIDREKLLRYLVSFRHHNEFHEQCVERIFNDL
LRFCQPEKLSVYARYTRRGGLDINPWRSNSDFVPSTTRLVRQ |
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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
- Van Lanen, S. G., Reader, J. S., Swairjo, M. A., de Crecy-Lagard, V., Lee, B., Iwata-Reuyl, D. (2005). "From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold." Proc Natl Acad Sci U S A 102:4264-4269. Pubmed: 15767583
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