Identification |
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Name: | 2-methylcitrate dehydratase |
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Synonyms: | Not Available |
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Gene Name: | prpD |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in 2-methylcitrate dehydratase activity |
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Specific Function: | Catalyzes the dehydration of 2-methylcitrate to 2- methyl-cis-aconitate. Also seems to be responsible for the residual aconitase activity of the acnAB-null strain |
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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: | |
1.02-Methylcitric acid | + | 1.0 | → | 1.0 | + | 1.0 |
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EcoCyc Reactions: | |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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2 iron, 2 sulfur cluster binding | 2-methylcitrate dehydratase activity | binding | carbon-oxygen lyase activity | catalytic activity | hydro-lyase activity | iron-sulfur cluster binding | lyase activity | metal cluster binding | Process |
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carboxylic acid metabolic process | cellular metabolic process | metabolic process | monocarboxylic acid metabolic process | organic acid metabolic process | oxoacid metabolic process | propionate catabolic process | propionate catabolic process, 2-methylcitrate cycle | propionate metabolic process |
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Gene Properties |
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Blattner: | b0334 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 7.55 |
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Left Sequence End | 350439 |
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Right Sequence End | 351890 |
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Gene Sequence: | >1452 bp
ATGTCAGCTCAAATCAACAACATCCGCCCGGAATTTGATCGTGAAATCGTTGATATCGTC
GATTACGTCATGAACTACGAAATCAGCTCTAAAGTGGCCTACGACACCGCACATTACTGC
CTGCTCGACACGCTCGGCTGCGGTCTGGAAGCTCTCGAATACCCGGCCTGTAAAAAACTG
CTGGGGCCAATTGTTCCCGGCACCGTCGTACCCAACGGCGTGCGCGTCCCCGGAACTCAG
TTCCAGCTCGACCCCGTCCAGGCGGCATTTAACATCGGCGCGATGATCCGCTGGCTCGAT
TTCAACGATACCTGGCTGGCGGCGGAGTGGGGCCATCCTTCCGACAACCTCGGCGGCATT
CTGGCAACGGCGGACTGGCTTTCGCGCAACGCGGTCGCCAGCGGCAAAGCGCCGTTGACC
ATGAAACAGGTGCTGACCGCAATGATCAAAGCCCATGAAATTCAGGGCTGCATCGCGCTG
GAAAACTCCTTTAACCGCGTCGGCCTCGACCACGTTCTGTTAGTGAAAGTGGCTTCCACC
GCCGTGGTCGCCGAAATGCTCGGCCTGACCCGCGAGGAAATTCTCAACGCCGTTTCGCTG
GCGTGGGTGGACGGTCAGTCGCTGCGCACCTATCGCCATGCGCCGAACACCGGCACGCGT
AAATCCTGGGCGGCGGGCGATGCCACTTCCCGCGCGGTACGTCTGGCACTGATGGCGAAA
ACGGGCGAAATGGGTTACCCGTCAGCCCTGACTGCGCCGGTGTGGGGCTTCTACGACGTC
TCCTTTAAAGGTGAATCGTTCCGCTTCCAGCGCCCGTACGGTTCCTACGTTATGGAAAAT
GTGCTGTTCAAAATCTCCTTCCCGGCGGAGTTCCACTCCCAGACGGCAGTTGAAGCAGCG
ATGACGCTCTATGAACAGATGCAGGCAGCAGGCAAAACGGCGGCGGATATCGAAAAAGTG
ACCATTCGCACCCACGAAGCCTGTATTCGCATCATCGACAAAAAAGGGCCGCTCAATAAC
CCGGCAGACCGCGATCACTGCATTCAGTACATGGTGGCGATCCCGCTGCTATTCGGGCGC
TTAACGGCGGCAGATTACGAGGACAACGTTGCGCAAGATAAACGCATTGACGCCCTGCGC
GAGAAGATCAATTGCTTTGAAGATCCGGCATTTACCGCTGACTACCACGACCCGGAAAAA
CGCGCCATCGCCAATGCCATTACCCTTGAGTTCACCGACGGCACACGATTTGAAGAAGTG
GTGGTGGAGTACCCCATTGGTCATGCTCGCCGCCGTCAGGATGGTATTCCGAAACTGGTC
GATAAATTCAAAATCAATCTCGCGCGCCAGTTCCCGACTCGCCAACAGCAGCGCATTCTG
GAGGTTTCTCTCGACAGAGCTCGCCTGGAACAGATGCCGGTCAATGAGTATCTCGACCTG
TACGTCATTTAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 483 |
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Protein Molecular Weight: | 53951 |
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Protein Theoretical pI: | 6 |
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PDB File: | 1SZQ |
Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >2-methylcitrate dehydratase
MSAQINNIRPEFDREIVDIVDYVMNYEISSKVAYDTAHYCLLDTLGCGLEALEYPACKKL
LGPIVPGTVVPNGVRVPGTQFQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGI
LATADWLSRNAVASGKAPLTMKQVLTAMIKAHEIQGCIALENSFNRVGLDHVLLVKVAST
AVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAK
TGEMGYPSALTAPVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAA
MTLYEQMQAAGKTAADIEKVTIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGR
LTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEKRAIANAITLEFTDGTRFEEV
VVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRARLEQMPVNEYLDL
YVI |
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References |
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External Links: | |
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General Reference: | - Blank, L., Green, J., Guest, J. R. (2002). "AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates." Microbiology 148:133-146. Pubmed: 11782506
- 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
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