Identification |
Name: |
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase |
Synonyms: |
- Protein envA
- UDP-3-O-acyl-GlcNAc deacetylase
|
Gene Name: |
lpxC |
Enzyme Class: |
|
Biological Properties |
General Function: |
Involved in UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity |
Specific Function: |
The key enzyme in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Degraded by FtsH; when the activity of FtsH is reduced too much lipid A and not enough phospholipids are made (both pathways use the same precursor), which is lethal |
Cellular Location: |
Cytoplasmic |
KEGG Pathways: |
|
KEGG Reactions: |
|
SMPDB Reactions: |
|
PseudoCyc/BioCyc Reactions: |
|
Complex Reactions: |
Not Available |
Transports: |
Not Available |
Metabolites: |
PAMDB ID | Name | View |
---|
PAMDB000012 | Acetic acid | MetaboCard | PAMDB000644 | UDP-3-O-(3-Hydroxymyristoyl)-N-acetylglucosamine | MetaboCard | PAMDB001696 | UDP-3-O-(3-Hydroxytetradecanoyl)-D-glucosamine | MetaboCard | PAMDB006332 | UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-α-D-glucosamine | MetaboCard | PAMDB000142 | Water | MetaboCard |
|
GO Classification: |
Function |
---|
catalytic activity | hydrolase activity | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity | Process |
---|
lipid A biosynthetic process | metabolic process | organophosphate metabolic process | phospholipid biosynthetic process | phospholipid metabolic process |
|
Gene Properties |
Locus tag: |
PA4406 |
Strand: |
- |
Entrez Gene ID: |
881292 |
Accession: |
NP_253096.1 |
GI: |
15599602 |
Sequence start: |
4938276 |
Sequence End: |
4939187 |
Sequence Length: |
911 |
Gene Sequence: |
>PA4406
ATGATCAAACAACGCACCTTGAAGAACATCATCCGGGCTACTGGCGTCGGTCTGCACTCGGGGGAAAAGGTTTACCTGACCCTGAAACCGGCGCCGGTGGACACCGGTATCGTGTTCTGCCGCACCGACCTGGATCCGGTCGTGGAAATCCCGGCCCGGGCCGAGAACGTCGGCGAAACCACCATGTCGACCACCCTGGTCAAGGGTGACGTCAAAGTGGATACGGTGGAGCACCTGCTCTCGGCCATGGCCGGCCTGGGTATCGACAACGCCTACGTCGAGCTGTCCGCTTCGGAAGTGCCGATCATGGATGGCAGCGCTGGTCCGTTCGTATTCCTGATCCAGTCCGCCGGATTGCAAGAGCAGGAAGCTGCCAAGAAGTTCATCCGCATCAAGCGCGAAGTCAGCGTGGAAGAGGGCGACAAGCGCGCCGTCTTCGTTCCGTTCGACGGCTTCAAGGTCAGCTTCGAGATCGATTTCGATCATCCGGTCTTCCGTGGTCGCACCCAGCAGGCCTCGGTCGATTTCTCCAGTACTTCCTTCGTCAAGGAGGTCAGCCGCGCCCGTACCTTCGGGTTCATGCGCGACATCGAGTACCTGCGTTCGCAGAACCTGGCACTCGGCGGTAGCGTGGAGAACGCGATCGTGGTCGACGAGAACCGCGTGCTCAACGAAGACGGCCTGCGTTACGAGGACGAGTTCGTCAAGCACAAGATCCTGGATGCCATCGGCGACCTGTATCTGCTCGGCAACAGTCTTATCGGCGAGTTCCGTGGCTTCAAGTCCGGCCATGCCCTGAACAACCAACTGCTGCGTACGTTGATCGCAGACAAGGATGCTTGGGAAGTGGTGACCTTCGAAGACGCGCGTACCGCGCCTATTTCCTATATGCGCCCGGCGGCGGCAGTGTAG |
Protein Properties |
Protein Residues: |
303 |
Protein Molecular Weight: |
33.4 kDa |
Protein Theoretical pI: |
5 |
Hydropathicity (GRAVY score): |
-0.066 |
Charge at pH 7 (predicted): |
-7.82 |
Protein Sequence: |
>PA4406
MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFCRTDLDPVVEIPARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEVPIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRAVFVPFDGFKVSFEIDFDHPVFRGRTQQASVDFSSTSFVKEVSRARTFGFMRDIEYLRSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYLLGNSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMRPAAAV |
References |
External Links: |
|
General Reference: |
PaperBLAST - Find papers about PA4406 and its homologs
|