| 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 |