Identification |
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Name: | Para-aminobenzoate synthase glutamine amidotransferase component II |
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Synonyms: | |
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Gene Name: | pabA |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in metabolic process |
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Specific Function: | Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine |
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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: | |
1.0 | + | 1.0 | → | 1.0L-Glutamic acid | + | 1.04-amino-4-deoxychorismate | + | 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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anthranilate synthase activity | carbon-carbon lyase activity | catalytic activity | lyase activity | oxo-acid-lyase activity | Process |
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biosynthetic process | cellular amino acid and derivative metabolic process | cellular amino acid metabolic process | cellular metabolic process | glutamine family amino acid metabolic process | glutamine metabolic process | metabolic process |
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Gene Properties |
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Blattner: | b3360 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 75.18 |
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Left Sequence End | 3488288 |
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Right Sequence End | 3488851 |
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Gene Sequence: | >564 bp
ATGTCCTTGATTAACACCAAAATTAAACCTTTTAAAAACCAGGCATTCAAAAACGGCGAA
TTCATCGAAATCACCGAAAAAGATACCGAAGGCCGCTGGAGCGTCTTCTTCTTCTACCCG
GCTGACTTTACTTTCGTATGCCCGACCGAACTGGGTGACGTTGCTGACCACTACGAAGAA
CTGCAGAAACTGGGCGTAGACGTATACGCAGTATCTACCGATACTCACTTCACCCACAAA
GCATGGCACAGCAGCTCTGAAACCATCGCTAAAATCAAATATGCGATGATCGGCGACCCG
ACTGGCGCCCTGACCCGTAACTTCGACAACATGCGTGAAGATGAAGGTCTGGCTGACCGT
GCGACCTTCGTTGTTGACCCGCAGGGTATCATCCAGGCAATCGAAGTTACCGCTGAAGGC
ATTGGCCGTGACGCGTCTGACCTGCTGCGTAAAATCAAAGCAGCACAGTACGTAGCTTCT
CACCCAGGTGAAGTTTGCCCGGCTAAATGGAAAGAAGGTGAAGCAACTCTGGCTCCGTCT
CTGGACCTGGTTGGTAAAATCTAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 187 |
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Protein Molecular Weight: | 20772 |
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Protein Theoretical pI: | 7 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Para-aminobenzoate synthase glutamine amidotransferase component II
MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAG
ISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLAN
PLTVTRYHSLVVEPDSLPACFDVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQL
LANFLHR |
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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
- Kaplan, J. B., Nichols, B. P. (1983). "Nucleotide sequence of Escherichia coli pabA and its evolutionary relationship to trp(G)D." J Mol Biol 168:451-468. Pubmed: 6350604
- Kawamukai, M., Matsuda, H., Fujii, W., Utsumi, R., Komano, T. (1989). "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli." J Bacteriol 171:4525-4529. Pubmed: 2546924
- Roux, B., Walsh, C. T. (1993). "p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA." Biochemistry 32:3763-3768. Pubmed: 8096767
- Tran, P. V., Bannor, T. A., Doktor, S. Z., Nichols, B. P. (1990). "Chromosomal organization and expression of Escherichia coli pabA." J Bacteriol 172:397-410. Pubmed: 2403545
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