| Identification |
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| Name: | 7-cyano-7-deazaguanine synthase |
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| Synonyms: | - 7-cyano-7-carbaguanine synthase
- PreQ(0) synthase
- Queuosine biosynthesis protein queC
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| Gene Name: | queC |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in argininosuccinate synthase activity |
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| Specific Function: | Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)) |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | |
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| KEGG Pathways: | |
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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: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0Adenosine diphosphate | + | 1.0 | + | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
1.07-carboxy-7-deazaguanine | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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| Complex Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Function |
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| adenyl nucleotide binding | | adenyl ribonucleotide binding | | argininosuccinate synthase activity | | ATP binding | | binding | | catalytic activity | | ligase activity | | ligase activity, forming carbon-nitrogen bonds | | nucleoside binding | | purine nucleoside binding | | Process |
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| arginine biosynthetic process | | arginine metabolic process | | cellular amino acid and derivative metabolic process | | cellular amino acid metabolic process | | cellular metabolic process | | glutamine family amino acid metabolic process | | metabolic process |
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| Gene Properties |
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| Blattner: | b0444 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 10.00 |
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| Left Sequence End | 464076 |
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| Right Sequence End | 464771 |
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| Gene Sequence: | >696 bp
ATGGATAATCGAGGCGAATTTTTGAATAACGTTGCTCAGGCACTGGGTCGCCCGCTGCGA
CTTGAACCGCAAGCAGAAGATGCGCCGCTTAACAACTATGCTAACGAGCGGCTTACCCAA
CTTAACCAACAGCAGCGCTGTGACGCGTTTATTCAGTTTGCCAGCGATGTTATGTTGACG
CGCTGTGAGCTGACCAGCGAGGCGAAGGCGGCAGAAGCTGCAATACGTCTGTGTAAAGAG
CTGGGAGATCAGTCGGTCGTGATTAGCGGTGACACGAGGCTGGAGGAATTGGGGATTAGC
GAACGTTTGCAGCAGGAATGCAATGCCGTTGTTTGGGATCCGGCGAAAGGTGCCGAGAAT
ATCTCGCAGGCAGAGCAGGCTAAAGTGGGTGTTGTGTATGCTGAATATGGTTTAACCGAA
TCGGGAGGCGTGGTTCTTTTTTCCGCCGCCGAGCGCGGGCGTTCATTGAGCCTGCTCCCG
GAATATTCTCTTTTTATCCTGCGTAAAAGCACTATCCTGCCGCGTGTAGCGCAACTCGCA
GAAAAATTGCATCAGAAAGCGCAGGCCGGTGAACGAATGCCTTCCTGCATTAACATCATT
AGCGGCCCCAGTTCAACGGCGGATATTGAGCTTATCAAAGTCGTCGGAGTTCATGGCCCG
GTGAAAGCGGTGTATCTGATTATTGAGGATTGTTGA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 231 |
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| Protein Molecular Weight: | 25514 |
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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: | >7-cyano-7-deazaguanine synthase
MKRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKV
LDVTLLNELAVSSLTRDSIPVPDYEPEADGIPNTFVPGRNILFLTLAAIYAYQVKAEAVI
TGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETPLMWIDKAETWALADYYGKLDL
VRNETLTCYNGFKGDGCGHCAACNLRANGLNHYLADKPTVMAAMKQKTGLR |
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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
- Gaur, R., Varshney, U. (2005). "Genetic analysis identifies a function for the queC (ybaX) gene product at an initial step in the queuosine biosynthetic pathway in Escherichia coli." J Bacteriol 187:6893-6901. Pubmed: 16199558
- 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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