| Identification |
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| Name: | Enterobactin synthase component E |
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| Synonyms: | - Enterochelin synthase E
- 2,3-dihydroxybenzoate-AMP ligase
- Dihydroxybenzoic acid-activating enzyme
- S-dihydroxybenzoyltransferase
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| Gene Name: | entE |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in catalytic activity |
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| Specific Function: | Activates the carboxylate group of 2,3-dihydroxy- benzoate (2,3-DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. Then, catalyzes the acylation of holo-entB with 2,3-DHB adenylate, preparing that molecule for amide bond formation with L-serine |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | - Biosynthesis of siderophore group nonribosomal peptides PW000760
- Enterobactin Biosynthesis PW002048
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| KEGG Pathways: | - Biosynthesis of siderophore group nonribosomal peptides ec01053
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| KEGG Reactions: | |
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| SMPDB Reactions: | |
6.0 | + | 3.0L-Serine | + | 3.0 | + | 3.0 | → | 6.0 | + | 1.0enterobactin | + | 6.0Pyrophosphate | + | 3.0 |
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1.0 | + | 1.0 | → | 1.0Pyrophosphate | + | 1.0 |
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1.0 | + | 1.0a holo-[EntB isochorismatase/aryl-carrier protein] | → | 1.0a 2,3-dihydroxybenzoyl-[EntB isochorismatase/aryl-carrier protein] | + | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | | | |
1.0 | + | 1.0holo-entB | → | 1.0 | + | 1.0acyl-holo-entB |
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| Metabolites: | |
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| GO Classification: | | Function |
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| (2,3-dihydroxybenzoyl)adenylate synthase activity | | adenylyltransferase activity | | catalytic activity | | nucleotidyltransferase activity | | transferase activity | | transferase activity, transferring phosphorus-containing groups | | Process |
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| cellular metabolic process | | cofactor metabolic process | | metabolic process | | siderophore biosynthetic process | | siderophore metabolic process |
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| Gene Properties |
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| Blattner: | b0594 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 13.48 |
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| Left Sequence End | 625293 |
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| Right Sequence End | 626903 |
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| Gene Sequence: | >1611 bp
ATGGAAATCACTAACCCGATACTCACCGGCTTCAACCCGGACCCGTCCCTGTGCCGCCAG
GGCGAGGACTACTACATCGCCACCTCGACCTTCGAGTGGTTCCCGGGCGTGCGCATCTAC
CACTCCCGTGACCTGAAAAACTGGTCGCTGGTCAGCACCCCGTTGGACCGCGTGTCGATG
CTGGACATGAAGGGCAACCCGGACTCCGGCGGCATCTGGGCGCCGTGCCTGAGCTACGCC
GACGGTAAATTCTGGCTGCTCTACACCGACGTGAAGATTGTCGACTCGCCGTGGAAAAAC
GGCCGCAACTTCCTCGTCACCGCGCCCTCCATCGAGGGGCCATGGAGCGAGCCAATCCCG
ATGGGCAACGGCGGGTTTGACCCGTCCCTGTTCCACGACGACGATGGCCGCAAATACTAT
ATCTACCGCCCGTGGGGGCCGCGCCACCACAGCAACCCGCACAACACCATCGTGTTACAG
GCGTTTGACCCGCAGACCGGCACGCTCTCGCCCGAGCGCAAAACGCTGTTTACCGGCACG
CCGCTCTGCTACACCGAAGGCGCGCACCTGTATCGCCACGCGGGATGGTACTACCTGATG
GCCGCCGAGGGCGGCACCAGCTACGAGCACGCCGTCGTGGTGCTGCGTTCCAAAAATATC
GACGGGCCGTACGAGCTGCACCCGGACGTAACGATGATGACCAGCTGGCACCTGCCGGAG
AACCCGCTGCAGAAGAGCGGCCACGGCTCGCTGCTGCAGACGCATACGGGTGAATGGTAC
ATGGCCTACCTCACCAGCCGCCCGCTGCGCCTGCCCGGCGTGCCGCTGCTGGCCTCCGGC
GGACGCGGCTACTGCCCGCTGGGGCGCGAGACCGGCATCGCCCGCATTGAATGGCGCGAC
GGCTGGCCGTACGTGGAAGGCGGCAAGCACGCGCAGCTGACCGTGAAAGGCCCGCAAGTA
GCCGAGCAGCCTGCAGCCGTTCCGGGCAACTGGCGGGACGATTTCGACGCCAGTTCGCTT
GACCCGGAGCTGCAGACCCTGCGCATTCCGTTCGACGACACCCTCGGCTCGCTCACCGCG
CGCCCGGGCTTCTTACGGCTCTATGGCAACGACTCGCTCAATTCGACCTTCACCCAATCG
ACCGTGGCGCGCCGCTGGCAGCACTTCGCCTTCCGGGCAGAAACGCGGATGGAGTTCTCG
CCGGTGCACTTCCAGCAGAGCGCGGGGCTGACCTGCTACTACAACAGCAAAAACTGGAGC
TACTGCTTTGTGGACTACGAGGAGGGACAGGGTAGAACCATCAAAGTTATCCAGCTCGAC
CACAACGTGCCGTCGTGGCCGCTGCACGAGCAGCCCATTCCGGTGCCGGAACATGCGGAG
AGCGTCTGGCTGCGGGTGGACGTGGATACGCTGGTCTACCGCTACAGCTACTCGTTTGAT
GGCGAGACGTGGCACACCGTGCCGGTGACGTATGAGGCGTGGAAGCTGTCGGACGACTAC
ATCGGCGGGCGCGGCTTCTTCACCGGCGCGTTTGTGGGCCTGCACTGCGAGGACATCAGC
GGCGACGGCTGCTACGCGGACTTCGACTACTTCACCTACGAGCCGGTCTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 536 |
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| Protein Molecular Weight: | 59112 |
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| Protein Theoretical pI: | 5 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Enterobactin synthase component E
MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDSIAVIDGERQLSYRELNQAADN
LACSLRRQGIKPGETALVQLGNVAELYITFFALLKLGVAPVLALFSHQRSELNAYASQIE
PALLIADRQHALFSGDDFLNTFVTEHSSIRVVQLLNDSGEHNLQDAINHPAEDFTATPSP
ADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSVEICQFTQQTRYLCAIPAAHNYAMSS
PGSLGVFLAGGTVVLAADPSATLCFPLIEKHQVNVTALVPPAVSLWLQALIEGESRAQLA
SLKLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDDSAEKIIHTQGYPMC
PDDEVWVADAEGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLISID
PEGYITVQGREKDQINRGGEKIAAEEIENLLLRHPAVIYAALVSMEDELMGEKSCAYLVV
KEPLRAVQVRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA |
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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
- Gehring, A. M., Bradley, K. A., Walsh, C. T. (1997). "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate." Biochemistry 36:8495-8503. Pubmed: 9214294
- 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
- Liu, J., Duncan, K., Walsh, C. T. (1989). "Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase." J Bacteriol 171:791-798. Pubmed: 2521622
- Saravani, G. A., Martin, D. R. (1990). "Opacity factor from group A streptococci is an apoproteinase." FEMS Microbiol Lett 56:35-39. Pubmed: 2110093
- Staab, J. F., Elkins, M. F., Earhart, C. F. (1989). "Nucleotide sequence of the Escherichia coli entE gene." FEMS Microbiol Lett 50:15-19. Pubmed: 2525505
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