Detail Information for IndEnz0002002190
IED ID IndEnz0002002190
Enzyme Type ID protease002190
Protein Name UDP-3-O-acyl-N-acetylglucosamine deacetylase
UDP-3-O-acyl-GlcNAc deacetylase
EC 3.5.1.108
Protein EnvA
UDP-3-O-
R-3-hydroxymyristoyl-N-acetylglucosamine deacetylase
Gene Name lpxC asmB envA b0096 JW0094
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA
Enzyme Length 305
Uniprot Accession Number P0A725
Absorption
Active Site ACT_SITE 265; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000305|PubMed:15705580, ECO:0000305|PubMed:24108127"
Activity Regulation ACTIVITY REGULATION: Regulation occurs at the protein level, via degradation of LpxC by the FtsH protease (PubMed:10048027, PubMed:16420369, PubMed:21193611, PubMed:23417489). Degradation is growth rate-dependent. LpxC is degraded rapidly during slow growth, probably to avoid toxic overproduction of lipopolysaccharides, but is highly stable under optimal growth conditions (PubMed:23417489). Increased amounts of LpxC are made under conditions that reduce the lipid A content of cells (PubMed:8824222). Inhibited by metal chelators such as EDTA and dipicolinic acid (DPA) and by high concentrations of Zn(2+) (PubMed:10026271). {ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:10048027, ECO:0000269|PubMed:16420369, ECO:0000269|PubMed:21193611, ECO:0000269|PubMed:23417489, ECO:0000269|PubMed:8824222}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate; Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:11148046, ECO:0000269|PubMed:15705580, ECO:0000269|PubMed:8530464, ECO:0000269|PubMed:8824222};
DNA Binding
EC Number 3.5.1.108
Enzyme Function FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:8530464, ECO:0000269|PubMed:8824222, ECO:0000269|Ref.7}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:8530464}.
nucleotide Binding
Features Active site (1); Beta strand (22); Chain (1); Helix (12); Metal binding (3); Mutagenesis (14); Natural variant (2); Turn (3)
Keywords 3D-structure;Direct protein sequencing;Hydrolase;Iron;Lipid A biosynthesis;Lipid biosynthesis;Lipid metabolism;Metal-binding;Reference proteome;Zinc
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Degraded by FtsH. {ECO:0000269|PubMed:10048027, ECO:0000269|PubMed:16420369, ECO:0000269|PubMed:21193611, ECO:0000269|PubMed:23417489}.
Signal Peptide
Structure 3D X-ray crystallography (4)
Cross Reference PDB 4IS9; 4ISA; 4MDT; 4MQY;
Mapped Pubmed ID 15690043; 16606699; 24561554;
Motif
Gene Encoded By
Mass 33,956
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 uM for UDP-3-O-myristoyl-N-acetylglucosamine (at 30 degrees Celsius) {ECO:0000269|PubMed:10026271}; KM=0.6 uM for UDP-3-O-myristoyl-N-acetylglucosamine (at 1 degree Celsius) {ECO:0000269|PubMed:10026271}; Note=kcat is 3.3 sec(-1) at 30 degrees Celsius. kcat is 0.09 sec(-1) at 1 degree Celsius. {ECO:0000269|PubMed:10026271};
Metal Binding METAL 79; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400"; METAL 238; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400"; METAL 242; /note="Zinc"; /evidence="ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400"
Rhea ID RHEA:67816
Cross Reference Brenda