ywpB

ywpB
168

ß-hydroxyacyl-(acyl carrier protein) dehydratase

Locus
BSU_36370
Molecular weight
14.63 kDa
Isoelectric point
9.36
Protein length
Gene length
Function
fatty acid biosynthesis
Product
β-hydroxyacyl-ACP dehydratase
Essential
yes
E.C.
4.2.1.59
Synonyms
ywpB, fabZ

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0764 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
3,743,732 → 3,744,157
Phenotypes of a mutant
essential PubMed
The protein
Catalyzed reaction/ biological activity
(3R)-hydroxyacyl-[ACP] --> (2E)-enoyl-[ACP] + H2O (according to UniProt)
Protein family
thioester dehydratase family (with YcsD, according to UniProt)
Structure
3D6X (PDB) (from Campylobacter jejuni, 45% identity, 67% similarity) PubMed
Paralogous protein(s)
Expression and Regulation
Operons
Genes
Description
Regulation
expressed in logarithmic phase PubMed
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ywpBmscL

2025-04-04 08:01:14

Jstuelk

113

5415340d20ac4baa52c66698ec0cc9bee9f29809

9C0AC698BF01AA86D7382CE0D746D52B12FABB4F

Biological materials
Mutant
MGNA-B265 (ywpB::erm), available at the NBRP B. subtilis, Japan
References
O'Reilly FJ, Graziadei A, Forbrig C, Bremenkamp R, Charles K, Lenz S, Elfmann C, Fischer L, Stülke J, Rappsilber JProtein complexes in cells by AI-assisted structural proteomics.Molecular systems biology. 2023 Feb 23; :e11544. PMID: 36815589
Kirkpatrick AS, Yokoyama T, Choi KJ, Yeo HJ Campylobacter jejuni fatty acid synthase II: structural and functional analysis of beta-hydroxyacyl-ACP dehydratase (FabZ). Biochemical and biophysical research communications. 2009 Mar 06; 380(2):407-12. doi:10.1016/j.bbrc.2009.01.115. PMID:19280690
Fujita Y, Matsuoka H, Hirooka K Regulation of fatty acid metabolism in bacteria. Molecular microbiology. 2007 Nov; 66(4):829-39. . PMID:17919287

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Time of last update: 2025-04-05 19:32:32

Author of last update: Jstuelk