3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
Details
- Name
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Kind
- protein
- Synonyms
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA
- 4.2.1.59
- Beta-hydroxydecanoyl thioester dehydrase
- Trans-2-decenoyl-[acyl-carrier-protein] isomerase
- Gene Name
- fabA
- UniProtKB Entry
- P0A6Q3Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0007677|3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase MVDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNFDKGYVEAELD INPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLP TAKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTASDLKVGLFQDTSAF
- Number of residues
- 172
- Molecular Weight
- 18968.945
- Theoretical pI
- 6.52
- GO Classification
- Functions3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity / 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity / trans-2-decenoyl-acyl-carrier-protein isomerase activityProcessesfatty acid biosynthetic process / lipid biosynthetic processComponentscytosol
- General Function
- Necessary for the introduction of cis unsaturation into fatty acids (PubMed:8910376). Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to (2E)-decenoyl-ACP and then its isomerization to (3Z)-decenoyl-ACP (PubMed:8910376). Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (PubMed:10629181, PubMed:7592873, PubMed:8910376). Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP (PubMed:8910376).
- Specific Function
- (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity
- Pfam Domain Function
- FabA (PF07977)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0020737|3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (fabA) ATGGTAGATAAACGCGAATCCTATACAAAAGAAGACCTTCTTGCCTCTGGTCGCGGTGAA CTGTTTGGCGCTAAAGGCCCGCAATTGCCAGCACCGAACATGCTGATGATGGACCGTGTG GTCAAAATGACCGAAACGGGTGGTAACTTCGACAAAGGGTATGTTGAAGCAGAACTGGAT ATCAATCCGGATCTGTGGTTCTTCGGATGCCACTTTATTGGCGATCCGGTTATGCCGGGA TGCCTGGGCCTGGACGCAATGTGGCAGCTGGTAGGGTTCTACCTCGGCTGGCTGGGCGGC GAAGGTAAAGGCCGCGCGCTGGGCGTTGGCGAAGTGAAATTCACTGGTCAGGTACTGCCG ACAGCGAAAAAAGTGACCTACCGTATTCACTTTAAACGCATTGTTAACCGTCGTCTGATT ATGGGCCTGGCGGATGGCGAAGTGCTGGTTGATGGTCGTCTGATCTATACCGCCAGCGAC CTGAAAGTCGGTCTGTTCCAGGATACGTCTGCCTTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A6Q3 UniProtKB Entry Name FABA_ECOLI GenBank Protein ID 1256744 GenBank Gene ID J03186 PDB ID(s) 1MKA, 1MKB, 4KEH KEGG ID ecj:JW0937 NCBI Gene ID 945568 - General References
- Cronan JE Jr, Li WB, Coleman R, Narasimhan M, de Mendoza D, Schwab JM: Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase. J Biol Chem. 1988 Apr 5;263(10):4641-6. [Article]
- Henry MF, Cronan JE Jr: A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding. Cell. 1992 Aug 21;70(4):671-9. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Rock CO, Tsay JT, Heath R, Jackowski S: Increased unsaturated fatty acid production associated with a suppressor of the fabA6(Ts) mutation in Escherichia coli. J Bacteriol. 1996 Sep;178(18):5382-7. [Article]
- Heath RJ, Rock CO: Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J Biol Chem. 1996 Nov 1;271(44):27795-801. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Zhang YM, Marrakchi H, Rock CO: The FabR (YijC) transcription factor regulates unsaturated fatty acid biosynthesis in Escherichia coli. J Biol Chem. 2002 May 3;277(18):15558-65. Epub 2002 Feb 21. [Article]
- Feng Y, Cronan JE: Complex binding of the FabR repressor of bacterial unsaturated fatty acid biosynthesis to its cognate promoters. Mol Microbiol. 2011 Apr;80(1):195-218. doi: 10.1111/j.1365-2958.2011.07564.x. Epub 2011 Feb 21. [Article]
- Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL: Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure. 1996 Mar 15;4(3):253-64. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2-Decenoyl N-acetyl cysteamine experimental unknown target Details