Detail Information for IndEnz0002006908
IED ID IndEnz0002006908
Enzyme Type ID protease006908
Protein Name 3-hydroxyacyl-
acyl-carrier-protein dehydratase FabZ
EC 4.2.1.59
3R
-hydroxymyristoyl-
acyl-carrier-protein dehydratase
3R
-hydroxymyristoyl-ACP dehydrase
17 kDa actomyosin component
Beta-hydroxyacyl-ACP dehydratase
Gene Name fabZ sefA yaeA b0180 JW0175
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MTTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSREA
Enzyme Length 151
Uniprot Accession Number P0A6Q6
Absorption
Active Site ACT_SITE 54; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627, ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631, ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458; Evidence={ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829; Evidence={ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635, ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462; Evidence={ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845; Evidence={ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861; Evidence={ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643, ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472; Evidence={ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877; Evidence={ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647, ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475; Evidence={ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893; Evidence={ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651, ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481; Evidence={ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909; Evidence={ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxy-(9Z)-hexadecenoyl-[ACP] = (2E,9Z)-hexadecadienoyl-[ACP] + H2O; Xref=Rhea:RHEA:54932, Rhea:RHEA-COMP:14036, Rhea:RHEA-COMP:14040, ChEBI:CHEBI:15377, ChEBI:CHEBI:138403, ChEBI:CHEBI:138407; Evidence={ECO:0000269|PubMed:8910376};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54933; Evidence={ECO:0000269|PubMed:8910376}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxy-5-methylhexanoyl-[ACP] = (2E)-5-methylhexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:55128, Rhea:RHEA-COMP:14095, Rhea:RHEA-COMP:14097, ChEBI:CHEBI:15377, ChEBI:CHEBI:78986, ChEBI:CHEBI:138610; Evidence={ECO:0000269|PubMed:10629181};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55129; Evidence={ECO:0000269|PubMed:10629181};
DNA Binding
EC Number 4.2.1.59
Enzyme Function FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (6); Chain (1); Helix (3); Mutagenesis (1); Turn (1)
Keywords 3D-structure;Cytoplasm;Direct protein sequencing;Lipid A biosynthesis;Lipid biosynthesis;Lipid metabolism;Lyase;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 6N3P;
Mapped Pubmed ID 15004283; 15690043; 16606699; 30872475;
Motif
Gene Encoded By
Mass 17,033
Kinetics
Metal Binding
Rhea ID RHEA:13097; RHEA:13098; RHEA:41808; RHEA:41809; RHEA:41828; RHEA:41829; RHEA:41844; RHEA:41845; RHEA:41860; RHEA:41861; RHEA:41876; RHEA:41877; RHEA:41892; RHEA:41893; RHEA:41908; RHEA:41909; RHEA:54932; RHEA:54933; RHEA:55128; RHEA:55129
Cross Reference Brenda