Holo-[acyl-carrier-protein] synthase
Details
- Name
- Holo-[acyl-carrier-protein] synthase
- Synonyms
- 2.7.8.7
- 4'-phosphopantetheinyl transferase AcpS
- Holo-ACP synthase
- ydcB
- Gene Name
- acpS
- Organism
- Bacillus subtilis (strain 168)
- Amino acid sequence
>lcl|BSEQ0019186|Holo-[acyl-carrier-protein] synthase MIYGIGLDITELKRIASMAGRQKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAF SKAFGTGIGRQLSFQDIEIRKDQNGKPYIICTKLSQAAVHVSITHTKEYAAAQVVIERLS S
- Number of residues
- 121
- Molecular Weight
- 13717.63
- Theoretical pI
- 10.08
- GO Classification
- Functionsholo-[acyl-carrier-protein] synthase activity / magnesium ion bindingProcessesfatty acid biosynthetic processComponentscytoplasm
- General Function
- Magnesium ion binding
- Specific Function
- Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl carrier protein of secondary metabolism.
- Pfam Domain Function
- ACPS (PF01648)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0019187|Holo-[acyl-carrier-protein] synthase (acpS) ATGATTTACGGCATTGGGCTGGACATTACCGAGCTTAAACGGATCGCCTCTATGGCTGGG CGCCAGAAAAGGTTTGCCGAGCGGATTTTGACGCGAAGCGAGCTTGACCAATACTATGAG CTTTCAGAGAAAAGAAAAAACGAATTTCTCGCGGGCAGATTCGCGGCAAAAGAAGCGTTC TCGAAAGCATTTGGCACCGGCATTGGGAGGCAGCTCAGCTTTCAGGACATTGAAATTAGG AAAGACCAAAATGGCAAGCCCTATATCATTTGTACGAAACTGAGCCAGGCCGCCGTTCAC GTATCGATCACTCATACAAAAGAATACGCTGCCGCGCAGGTTGTGATTGAAAGGTTGTCA AGCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P96618 UniProtKB Entry Name ACPS_BACSU GenBank Protein ID 1881272 GenBank Gene ID AB001488 - General References
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- Mootz HD, Finking R, Marahiel MA: 4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J Biol Chem. 2001 Oct 5;276(40):37289-98. Epub 2001 Aug 6. [Article]
- Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS: Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure. 2000 Aug 15;8(8):883-95. [Article]