UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (P0A725)

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
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0UDP-3-O-(3-Hydroxymyristoyl)-N-acetylglucosamine ↔ 1.0Acetic acid + 1.0UDP-3-O-(3-Hydroxytetradecanoyl)-D-glucosamine
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-α-D-glucosamine + 1.0Water → 1.0Acetic acid + 1.0UDP-3-O-(3-Hydroxytetradecanoyl)-D-glucosamine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0UDP-3-O-(3-Hydroxymyristoyl)-N-acetylglucosamine ↔ 1.0Acetic acid + 1.0UDP-3-O-(3-Hydroxytetradecanoyl)-D-glucosamine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0UDP-3-O-(3-Hydroxymyristoyl)-N-acetylglucosamine + 1.0Water → 1.0UDP-3-O-(3-Hydroxytetradecanoyl)-D-glucosamine + 1.0Acetic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00042Acetic acidMetaboCard
ECMDB04164UDP-3-O-(3-Hydroxymyristoyl)-N-acetylglucosamineMetaboCard
ECMDB21292UDP-3-O-(3-Hydroxytetradecanoyl)-D-glucosamineMetaboCard
ECMDB24215UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-α-D-glucosamineMetaboCard
ECMDB00494WaterMetaboCard
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
Blattner:b0096
Gene OrientationClockwise
Centisome Percentage:2.30
Left Sequence End106557
Right Sequence End107474
Gene Sequence:
>918 bp
ATGATCAAACAAAGGACACTTAAACGTATCGTTCAGGCGACGGGTGTCGGTTTACATACC
GGCAAGAAAGTCACCCTGACGTTACGCCCTGCGCCGGCCAACACCGGGGTCATCTATCGT
CGCACCGACTTGAATCCACCGGTAGATTTCCCGGCCGATGCCAAATCTGTGCGTGATACC
ATGCTCTGTACGTGTCTGGTCAACGAGCATGATGTACGGATTTCAACCGTAGAGCACCTC
AATGCTGCTCTCGCGGGCTTGGGCATCGATAACATTGTTATCGAAGTTAACGCGCCGGAA
ATCCCGATCATGGACGGCAGCGCCGCTCCGTTTGTATACCTGCTGCTTGACGCCGGTATC
GACGAGTTGAACTGCGCCAAAAAATTTGTTCGCATCAAAGAGACTGTTCGTGTCGAAGAT
GGCGATAAGTGGGCTGAATTTAAGCCGTACAATGGTTTTTCGCTGGATTTCACCATCGAT
TTTAACCATCCGGCTATTGATTCCAGCAACCAGCGCTATGCGATGAACTTCTCCGCTGAT
GCGTTTATGCGCCAGATCAGCCGTGCGCGTACGTTCGGTTTCATGCGTGATATCGAATAT
CTGCAGTCCCGTGGTTTGTGCCTGGGCGGCAGCTTCGATTGTGCCATCGTTGTTGACGAT
TATCGCGTACTGAACGAAGACGGCCTGCGTTTTGAAGACGAATTTGTGCGTCACAAAATG
CTCGATGCGATCGGTGACTTGTTCATGTGTGGTCACAATATTATTGGTGCATTTACCGCT
TATAAATCCGGTCATGCACTGAATAACAAACTGCTGCAGGCTGTCCTGGCGAAACAGGAA
GCCTGGGAATATGTGACCTTCCAGGACGACGCAGAACTGCCGTTGGCCTTCAAAGCGCCT
TCAGCTGTACTGGCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:305
Protein Molecular Weight:33956
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase
MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDT
MLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGI
DELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSAD
AFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKM
LDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAP
SAVLA
References
External Links:
ResourceLink
Uniprot ID:P0A725
Uniprot Name:LPXC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321977
Ecogene ID:EG10265
Ecocyc:EG10265
ColiBase:b0096
Kegg Gene:b0096
EchoBASE ID:EB0261
CCDB:LPXC_ECOLI
BacMap:16128089
General Reference:
  • Beall, B., Lutkenhaus, J. (1987). "Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli." J Bacteriol 169:5408-5415. Pubmed: 2824434
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kloser, A. W., Laird, M. W., Misra, R. (1996). "asmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC)." J Bacteriol 178:5138-5143. Pubmed: 8752330
  • Ogura, T., Inoue, K., Tatsuta, T., Suzaki, T., Karata, K., Young, K., Su, L. H., Fierke, C. A., Jackman, J. E., Raetz, C. R., Coleman, J., Tomoyasu, T., Matsuzawa, H. (1999). "Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli." Mol Microbiol 31:833-844. Pubmed: 10048027
  • Yi, Q. M., Lutkenhaus, J. (1985). "The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli." Gene 36:241-247. Pubmed: 3000876
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901