Identification |
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Name: | Holo-[acyl-carrier-protein] synthase |
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Synonyms: | - Holo-ACP synthase
- 4'-phosphopantetheinyl transferase AcpS
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Gene Name: | acpS |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in magnesium ion binding |
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Specific Function: | Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein |
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Cellular Location: | Cytoplasm (Probable) |
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SMPDB Pathways: | - Pantothenate and CoA biosynthesis PW000828
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KEGG Pathways: | - Pantothenate and CoA biosynthesis ec00770
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KEGG Reactions: | |
1.0 | + | 1.0Apo-[acyl-carrier-protein] | ↔ | 1.0 | + | 1.0Acyl-carrier protein | + | 1.0Acyl-carrier protein |
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Complex Reactions: | |
1.0apoprotein [acyl carrier protein] | + | 1.0 | → | 1.0acyl carrier protein | + | 1.0 | + | 1.0 |
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1.0CoA-(4'-phosphopantetheine) | + | 1.0apo-[acyl-carrier-protein] | → | 1.0 | + | 1.0holo-[acyl-carrier-protein] |
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Metabolites: | |
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GO Classification: | Function |
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binding | catalytic activity | cation binding | holo-[acyl-carrier-protein] synthase activity | ion binding | magnesium ion binding | metal ion binding | phosphotransferase activity, for other substituted phosphate groups | transferase activity | transferase activity, transferring phosphorus-containing groups | Process |
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biosynthetic process | carboxylic acid metabolic process | cellular metabolic process | fatty acid biosynthetic process | fatty acid metabolic process | macromolecule biosynthetic process | metabolic process | monocarboxylic acid metabolic process | organic acid metabolic process | oxoacid metabolic process |
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Gene Properties |
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Blattner: | b2563 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 58.16 |
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Left Sequence End | 2698640 |
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Right Sequence End | 2699020 |
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Gene Sequence: | >381 bp
ATGGCAATATTAGGTTTAGGCACGGATATTGTGGAGATCGCTCGCATCGAAGCGGTGATC
GCCCGATCCGGTGATCGCCTGGCACGCCGCGTATTAAGCGATAACGAATGGGCTATCTGG
AAAACGCACCACCAGCCGGTGCGTTTTCTGGCGAAGCGTTTTGCTGTGAAAGAAGCCGCA
GCAAAAGCGTTTGGCACCGGGATCCGCAATGGTCTGGCGTTTAATCAATTTGAAGTATTC
AATGATGAGCTCGGCAAACCACGGCTACGGCTATGGGGCGAGGCATTAAAACTGGCGGAA
AAGCTGGGCGTTGCAAATATGCATGTAACGCTGGCAGATGAGCGGCACTATGCTTGTGCC
ACGGTAATTATTGAAAGTTAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 126 |
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Protein Molecular Weight: | 14052 |
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Protein Theoretical pI: | 10 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Holo-[acyl-carrier-protein] synthase
MAILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWKTHHQPVRFLAKRFAVKEAA
AKAFGTGIRNGLAFNQFEVFNDELGKPRLRLWGEALKLAEKLGVANMHVTLADERHYACA
TVIIES |
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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
- Flugel, R. S., Hwangbo, Y., Lambalot, R. H., Cronan, J. E. Jr, Walsh, C. T. (2000). "Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli." J Biol Chem 275:959-968. Pubmed: 10625633
- 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
- Lam, H. M., Tancula, E., Dempsey, W. B., Winkler, M. E. (1992). "Suppression of insertions in the complex pdxJ operon of Escherichia coli K-12 by lon and other mutations." J Bacteriol 174:1554-1567. Pubmed: 1537800
- Lambalot, R. H., Walsh, C. T. (1995). "Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase." J Biol Chem 270:24658-24661. Pubmed: 7559576
- Takiff, H. E., Baker, T., Copeland, T., Chen, S. M., Court, D. L. (1992). "Locating essential Escherichia coli genes by using mini-Tn10 transposons: the pdxJ operon." J Bacteriol 174:1544-1553. Pubmed: 1537799
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