| Identification |
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| Name: | Riboflavin biosynthesis protein ribD |
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| Synonyms: | - Diaminohydroxyphosphoribosylaminopyrimidine deaminase
- DRAP deaminase
- Riboflavin-specific deaminase
- 5-amino-6-(5-phosphoribosylamino)uracil reductase
- HTP reductase
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| Gene Name: | ribD |
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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: | Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5'-phosphate |
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| Cellular Location: | Cytoplasmic |
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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 | + | 1.0 | + | 1.0NADPH | + | 1.0 | → | 1.0 | + | 1.05-Amino-6-(5'-phosphoribitylamino)uracil | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | | | |
1.0 | + | 1.0 | → | 1.05-amino-6-(5-phospho-D-ribosylamino)uracil | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Function |
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| 5-amino-6-(5-phosphoribosylamino)uracil reductase activity | | binding | | catalytic activity | | cation binding | | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity | | hydrolase activity | | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines | | ion binding | | metal ion binding | | NADP or NADPH 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 | | transition metal ion binding | | zinc ion binding | | Process |
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| metabolic process | | nitrogen compound metabolic process | | oxidation reduction | | riboflavin biosynthetic process | | riboflavin metabolic process |
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| Gene Properties |
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| Blattner: | b0414 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 9.33 |
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| Left Sequence End | 432679 |
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| Right Sequence End | 433782 |
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| Gene Sequence: | >1104 bp
ATGAGTGACAGCCAGACGCTGGTGGTAAAACTCGGCACCAGTGTGCTAACAGGCGGATCG
CGCCGTCTGAACCGTGCCCATATCGTTGAACTTGTTCGCCAGTGCGCGCAGTTACATGCC
GCCGGGCATCGGATTGTTATTGTGACGTCGGGCGCGATCGCCGCCGGACGTGAGCACCTG
GGTTACCCGGAACTGCCAGCGACCATCGCCTCGAAACAACTGCTGGCGGCGGTAGGGCAG
AGTCGACTGATTCAACTGTGGGAACAGCTGTTTTCGATTTATGGCATTCACGTCGGGCAA
ATGCTGCTGACCCGTGCTGATATGGAAGACCGTGAACGCTTCCTGAACGCCCGCGACACC
CTGCGAGCGTTGCTCGATAACAATATCGTTCCGGTAATCAATGAGAACGATGCTGTCGCT
ACGGCAGAGATTAAGGTCGGCGATAACGATAACCTTTCTGCGCTGGCGGCGATTCTTGCG
GGTGCCGATAAACTGTTGCTGCTGACCGATCAAAAAGGTTTGTATACCGCTGACCCGCGC
AGCAATCCGCAGGCAGAACTGATTAAAGATGTTTACGGCATTGATGACGCACTGCGCGCG
ATTGCCGGTGACAGCGTTTCAGGCCTCGGAACTGGCGGCATGAGTACCAAATTGCAGGCC
GCTGACGTGGCTTGCCGTGCGGGTATCGACACCATTATTGCCGCGGGCAGCAAGCCGGGC
GTTATTGGTGATGTGATGGAAGGCATTTCCGTCGGTACGCTGTTCCATGCCCAGGCGACT
CCGCTTGAAAACCGTAAACGCTGGATTTTCGGTGCGCCGCCGGCGGGTGAAATCACGGTA
GATGAAGGGGCAACTGCCGCCATTCTGGAACGCGGCAGCTCCCTGTTGCCGAAAGGCATT
AAAAGCGTGACTGGCAATTTCTCGCGTGGTGAAGTCATCCGCATTTGCAACCTCGAAGGC
CGCGATATCGCCCACGGCGTCAGTCGTTACAACAGCGATGCATTACGCCGTATTGCCGGA
CACCACTCGCAAGAAATTGATGCAATACTGGGATATGAATACGGCCCGGTTGCCGTTCAC
CGTGATGACATGATTACCCGTTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 367 |
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| Protein Molecular Weight: | 40338 |
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| Protein Theoretical pI: | 8 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Riboflavin biosynthesis protein ribD
MQDEYYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAG
EKAKGATAYVTLEPCSHHGRTPPCCDALIAAGVARVVASMQDPNPQVAGRGLYRLQQAGI
DVSHGLMMSEAEQLNKGFLKRMRTGFPYIQLKLGASLDGRTAMASGESQWITSPQARRDV
QLLRAQSHAILTSSATVLADDPALTVRWSELDEQTQALYPQQNLRQPIRIVIDSQNRVTP
VHRIVQQPGETWFARTQEDSREWPETVRTLLIPEHKGHLDLVVLMMQLGKQQINSIWVEA
GPTLAGALLQAGLVDELIVYIAPKLLGSDARGLCTLPGLEKLADAPQFKFKEIRHVGPDV
CLHLVGA |
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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
- Richter, G., Fischer, M., Krieger, C., Eberhardt, S., Luttgen, H., Gerstenschlager, I., Bacher, A. (1997). "Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis." J Bacteriol 179:2022-2028. Pubmed: 9068650
- Stenmark, P., Moche, M., Gurmu, D., Nordlund, P. (2007). "The crystal structure of the bifunctional deaminase/reductase RibD of the riboflavin biosynthetic pathway in Escherichia coli: implications for the reductive mechanism." J Mol Biol 373:48-64. Pubmed: 17765262
- Taura, T., Ueguchi, C., Shiba, K., Ito, K. (1992). "Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation." Mol Gen Genet 234:429-432. Pubmed: 1406588
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