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Protein

UDP-3-O-acyl-N-acetylglucosamine deacetylase

Gene

lpxC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H2O = UDP-3-O-((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation1 Publication

Pathwayi: lipid IV(A) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
  2. UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
  3. no protein annotated in this organism
  4. UDP-2,3-diacylglucosamine hydrolase (lpxH)
  5. Lipid-A-disaccharide synthase (lpxB)
  6. Tetraacyldisaccharide 4'-kinase (lpxK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi78 – 781Zinc; via tele nitrogenUniRule annotation
Metal bindingi237 – 2371Zinc; via tele nitrogenUniRule annotation
Metal bindingi241 – 2411ZincUniRule annotation
Active sitei264 – 2641Proton donorUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • lipid A biosynthetic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.108. 5087.
UniPathwayiUPA00359; UER00478.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-3-O-acyl-N-acetylglucosamine deacetylaseUniRule annotation (EC:3.5.1.108UniRule annotation1 Publication)
Short name:
UDP-3-O-acyl-GlcNAc deacetylaseUniRule annotation
Alternative name(s):
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylaseUniRule annotation
Gene namesi
Name:lpxCUniRule annotation
Synonyms:envA
Ordered Locus Names:PA4406
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4406.

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303UDP-3-O-acyl-N-acetylglucosamine deacetylasePRO_0000191945Add
BLAST

Proteomic databases

PaxDbiP47205.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA4406.

Chemistry

BindingDBiP47205.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi11 – 166Combined sources
Turni18 – 203Combined sources
Beta strandi23 – 297Combined sources
Beta strandi37 – 415Combined sources
Beta strandi44 – 463Combined sources
Beta strandi48 – 514Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 684Combined sources
Beta strandi71 – 744Combined sources
Helixi77 – 859Combined sources
Beta strandi91 – 999Combined sources
Beta strandi105 – 1073Combined sources
Helixi108 – 11710Combined sources
Beta strandi119 – 1257Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi150 – 1589Combined sources
Helixi163 – 1653Combined sources
Beta strandi170 – 1756Combined sources
Helixi178 – 1847Combined sources
Turni185 – 1873Combined sources
Beta strandi191 – 1933Combined sources
Helixi194 – 1963Combined sources
Helixi197 – 2037Combined sources
Turni211 – 2133Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi219 – 2224Combined sources
Helixi233 – 24715Combined sources
Beta strandi250 – 26112Combined sources
Helixi264 – 27613Combined sources
Helixi278 – 2803Combined sources
Beta strandi281 – 2844Combined sources
Helixi289 – 2913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VESX-ray1.90A/B/C1-299[»]
3P3EX-ray1.28A1-299[»]
3U1YX-ray2.00A/B1-299[»]
3UHMX-ray1.26A1-299[»]
4FW3X-ray2.35A/B/C/D1-299[»]
4FW4X-ray2.19A/B/C/D1-299[»]
4FW5X-ray1.99A/B/C/D1-299[»]
4FW6X-ray1.83A/B/C/D1-299[»]
4FW7X-ray1.70A/B/C/D1-299[»]
4J3DX-ray2.00A/B1-297[»]
4LCFX-ray1.60A1-299[»]
4LCGX-ray1.57A1-299[»]
4LCHX-ray1.60A1-299[»]
4OKGX-ray2.06A/B1-299[»]
5DRQX-ray1.63A1-299[»]
5DRRX-ray1.59A1-299[»]
ProteinModelPortaliP47205.
SMRiP47205. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47205.

Family & Domainsi

Sequence similaritiesi

Belongs to the LpxC family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C7C. Bacteria.
COG0774. LUCA.
HOGENOMiHOG000256663.
InParanoidiP47205.
KOiK02535.
OMAiNSMLVKA.
OrthoDBiEOG6PGK74.
PhylomeDBiP47205.

Family and domain databases

Gene3Di3.30.1700.10. 1 hit.
3.30.230.20. 1 hit.
HAMAPiMF_00388. LpxC.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR004463. UDP-acyl_GlcNac_deAcase.
IPR011334. UDP-acyl_GlcNac_deAcase_C.
IPR015870. UDP-acyl_N-AcGlcN_deAcase_N.
[Graphical view]
PfamiPF03331. LpxC. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
TIGRFAMsiTIGR00325. lpxC. 1 hit.

Sequencei

Sequence statusi: Complete.

P47205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKQRTLKNI IRATGVGLHS GEKVYLTLKP APVDTGIVFC RTDLDPVVEI
60 70 80 90 100
PARAENVGET TMSTTLVKGD VKVDTVEHLL SAMAGLGIDN AYVELSASEV
110 120 130 140 150
PIMDGSAGPF VFLIQSAGLQ EQEAAKKFIR IKREVSVEEG DKRAVFVPFD
160 170 180 190 200
GFKVSFEIDF DHPVFRGRTQ QASVDFSSTS FVKEVSRART FGFMRDIEYL
210 220 230 240 250
RSQNLALGGS VENAIVVDEN RVLNEDGLRY EDEFVKHKIL DAIGDLYLLG
260 270 280 290 300
NSLIGEFRGF KSGHALNNQL LRTLIADKDA WEVVTFEDAR TAPISYMRPA

AAV
Length:303
Mass (Da):33,435
Last modified:December 8, 2000 - v2
Checksum:i454403711DCC9B24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19797 Genomic DNA. Translation: AAA95994.2.
U67855 Genomic DNA. Translation: AAC44974.1.
AE004091 Genomic DNA. Translation: AAG07794.1.
PIRiG83093.
RefSeqiNP_253096.1. NC_002516.2.
WP_003094111.1. NZ_ASJY01000726.1.

Genome annotation databases

EnsemblBacteriaiAAG07794; AAG07794; PA4406.
GeneIDi881292.
KEGGipae:PA4406.
PATRICi19843537. VBIPseAer58763_4615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19797 Genomic DNA. Translation: AAA95994.2.
U67855 Genomic DNA. Translation: AAC44974.1.
AE004091 Genomic DNA. Translation: AAG07794.1.
PIRiG83093.
RefSeqiNP_253096.1. NC_002516.2.
WP_003094111.1. NZ_ASJY01000726.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VESX-ray1.90A/B/C1-299[»]
3P3EX-ray1.28A1-299[»]
3U1YX-ray2.00A/B1-299[»]
3UHMX-ray1.26A1-299[»]
4FW3X-ray2.35A/B/C/D1-299[»]
4FW4X-ray2.19A/B/C/D1-299[»]
4FW5X-ray1.99A/B/C/D1-299[»]
4FW6X-ray1.83A/B/C/D1-299[»]
4FW7X-ray1.70A/B/C/D1-299[»]
4J3DX-ray2.00A/B1-297[»]
4LCFX-ray1.60A1-299[»]
4LCGX-ray1.57A1-299[»]
4LCHX-ray1.60A1-299[»]
4OKGX-ray2.06A/B1-299[»]
5DRQX-ray1.63A1-299[»]
5DRRX-ray1.59A1-299[»]
ProteinModelPortaliP47205.
SMRiP47205. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4406.

Chemistry

BindingDBiP47205.
ChEMBLiCHEMBL3855.

Proteomic databases

PaxDbiP47205.

Protocols and materials databases

DNASUi881292.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07794; AAG07794; PA4406.
GeneIDi881292.
KEGGipae:PA4406.
PATRICi19843537. VBIPseAer58763_4615.

Organism-specific databases

PseudoCAPiPA4406.

Phylogenomic databases

eggNOGiENOG4105C7C. Bacteria.
COG0774. LUCA.
HOGENOMiHOG000256663.
InParanoidiP47205.
KOiK02535.
OMAiNSMLVKA.
OrthoDBiEOG6PGK74.
PhylomeDBiP47205.

Enzyme and pathway databases

UniPathwayiUPA00359; UER00478.
BRENDAi3.5.1.108. 5087.

Miscellaneous databases

EvolutionaryTraceiP47205.

Family and domain databases

Gene3Di3.30.1700.10. 1 hit.
3.30.230.20. 1 hit.
HAMAPiMF_00388. LpxC.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR004463. UDP-acyl_GlcNac_deAcase.
IPR011334. UDP-acyl_GlcNac_deAcase_C.
IPR015870. UDP-acyl_N-AcGlcN_deAcase_N.
[Graphical view]
PfamiPF03331. LpxC. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
TIGRFAMsiTIGR00325. lpxC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Levesque R.C.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway."
    Hyland S.A., Eveland S.S., Anderson M.S.
    J. Bacteriol. 179:2029-2037(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    Strain: ATCC 27853 / DSM 1117 / JCM 6119 / LMG 6395 / NCIMB 12469.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  4. "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1 chromosome."
    Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J., Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.
    Microbiology 142:79-86(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiLPXC_PSEAE
AccessioniPrimary (citable) accession number: P47205
Secondary accession number(s): P97050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 8, 2000
Last modified: May 11, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.