Identification |
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Name: | Propionate kinase |
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Synonyms: | Not Available |
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Gene Name: | tdcD |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in kinase activity |
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Specific Function: | ATP + propanoate = ADP + propanoyl phosphate |
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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: | |
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SMPDB Reactions: | |
1.0Adenosine diphosphate | + | 1.0propanoyl phosphate | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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EcoCyc Reactions: | |
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Metabolites: | |
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GO Classification: | Component |
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cell part | intracellular | Function |
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catalytic activity | kinase activity | phosphotransferase activity, carboxyl group as acceptor | transferase activity | transferase activity, transferring phosphorus-containing groups | Process |
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cellular metabolic process | metabolic process | organic acid metabolic process | phosphate metabolic process | phosphorus metabolic process | phosphorylation |
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Gene Properties |
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Blattner: | b3115 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 70.27 |
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Left Sequence End | 3260474 |
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Right Sequence End | 3261682 |
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Gene Sequence: | >1209 bp
ATGGCCTTTTCTCAAGCGGTTAGCGGATTAAACGCTGCCGCCACCAACCTCGATGTTATT
GGCAACAATATCGCCAACTCCGCCACCTACGGCTTTAAATCAGGCACGGCCTCTTTTGCC
GATATGTTTGCCGGTTCGAAAGTGGGACTGGGGGTAAAAGTTGCCGGTATCACTCAGGAC
TTTACCGATGGCACGACCACCAACACCGGGCGAGGTCTGGACGTTGCTATCAGCCAGAAC
GGTTTTTTCCGTCTGGTAGACAGCAACGGTTCGGTGTTCTACAGCCGTAACGGACAATTT
AAGCTGGATGAAAACCGTAACCTGGTGAATATGCAAGGTTTACAGCTGACGGGTTACCCG
GCAACCGGTACGCCGCCGACTATTCAGCAAGGGGCGAATCCGACCAATATTTCGATCCCG
AATACCCTGATGGCAGCGAAAACTACCACCACGGCATCGATGCAGATCAACCTGAATTCC
AGTGATCCGCTTCCTACTGTTACGCCATTCAGCGCCAGCAATGCGGATAGCTATAACAAA
AAAGGTTCGGTGACTGTTTTCGACAGTCAGGGTAATGCTCATGACATGAGCGTCTACTTT
GTGAAGACCGGGGATAATAACTGGCAGGTCTACACCCAGGATAGCAGTGATCCAAACAGC
ATTGCGAAGACAGCGACAACACTGGAATTTAATGCTAATGGCACATTAGTGGATGGTGCG
ATGGCGAATAATATCGCAACCGGCGCAATTAACGGTGCAGAACCCGCCACGTTTAGTCTG
AGCTTCCTCAACTCCATGCAGCAAAATACCGGCGCTAACAATATTGTGGCAACCACCCAG
AACGGCTACAAACCGGGCGATCTGGTGAGTTATCAAATCAATGATGACGGTACGGTTGTC
GGCAACTATTCCAACGAACAAACCCAACTGCTGGGGCAGATTGTACTGGCGAACTTTGCC
AACAACGAAGGTCTGGCATCCGAAGGCGACAACGTCTGGTCTGCGACGCAATCTTCTGGC
GTGGCGCTGTTGGGGACAGCCGGGACGGGAAACTTTGGCACCCTGACCAACGGTGCGCTG
GAAGCGTCCAACGTCGATCTCAGTAAAGAACTGGTCAATATGATCGTTGCCCAGCGTAAC
TATCAGTCTAACGCCCAGACCATCAAAACCCAGGACCAGATCCTCAACACGCTGGTTAAC
TTACGCTAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 402 |
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Protein Molecular Weight: | 43384 |
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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: | >Propionate kinase
MNEFPVVLVINCGSSSIKFSVLDASDCEVLMSGIADGINSENAFLSVNGGEPAPLAHHSY
EGALKAIAFELEKRNLNDSVALIGHRIAHGGSIFTESAIITDEVIDNIRRVSPLAPLHNY
ANLSGIESAQQLFPGVTQVAVFDTSFHQTMAPEAYLYGLPWKYYEELGVRRYGFHGTSHR
YVSQRAHSLLNLAEDDSGLVVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDV
DFGAMSWVASQTNQSLGDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERAQLAIKTF
VHRIARHIAGHAASLRRLDGIIFTGGIGENSSLIRRLVMEHLAVLGLEIDTEMNNRSNSC
GERIVSSENARVICAVIPTNEEKMIALDAIHLGKVNAPAEFA |
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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
- Goss, T. J., Schweizer, H. P., Datta, P. (1988). "Molecular characterization of the tdc operon of Escherichia coli K-12." J Bacteriol 170:5352-5359. Pubmed: 3053659
- Grundy, F. J., Waters, D. A., Allen, S. H., Henkin, T. M. (1993). "Regulation of the Bacillus subtilis acetate kinase gene by CcpA." J Bacteriol 175:7348-7355. Pubmed: 8226682
- 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
- Hesslinger, C., Fairhurst, S. A., Sawers, G. (1998). "Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate." Mol Microbiol 27:477-492. Pubmed: 9484901
- Schweizer, H. P., Datta, P. (1989). "The complete nucleotide sequence of the tdc region of Escherichia coli." Nucleic Acids Res 17:3994. Pubmed: 2660107
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