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Protein

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

Gene

lpxC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Metal bindingi78Zinc; via tele nitrogenUniRule annotation1
Metal bindingi237Zinc; via tele nitrogenUniRule annotation1
Metal bindingi241ZincUniRule annotation1
Active sitei264Proton donorUniRule annotation1

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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4406.

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001919451 – 303UDP-3-O-acyl-N-acetylglucosamine deacetylaseAdd BLAST303

Proteomic databases

PaxDbiP47205.
PRIDEiP47205.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA4406.

Chemistry databases

BindingDBiP47205.

Structurei

Secondary structure

1303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi11 – 16Combined sources6
Turni18 – 20Combined sources3
Beta strandi23 – 29Combined sources7
Beta strandi37 – 41Combined sources5
Beta strandi44 – 46Combined sources3
Beta strandi48 – 51Combined sources4
Helixi54 – 56Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi61 – 63Combined sources3
Beta strandi65 – 68Combined sources4
Beta strandi71 – 74Combined sources4
Helixi77 – 85Combined sources9
Beta strandi91 – 99Combined sources9
Beta strandi105 – 107Combined sources3
Helixi108 – 117Combined sources10
Beta strandi119 – 125Combined sources7
Beta strandi128 – 131Combined sources4
Beta strandi135 – 139Combined sources5
Beta strandi142 – 147Combined sources6
Beta strandi150 – 158Combined sources9
Helixi163 – 165Combined sources3
Beta strandi170 – 175Combined sources6
Helixi178 – 184Combined sources7
Turni185 – 187Combined sources3
Beta strandi191 – 193Combined sources3
Helixi194 – 196Combined sources3
Helixi197 – 203Combined sources7
Turni211 – 213Combined sources3
Beta strandi214 – 217Combined sources4
Beta strandi219 – 222Combined sources4
Helixi233 – 247Combined sources15
Beta strandi250 – 261Combined sources12
Helixi264 – 276Combined sources13
Helixi278 – 280Combined sources3
Beta strandi281 – 284Combined sources4
Helixi289 – 291Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
PhylomeDBiP47205.

Family and domain databases

Gene3Di3.30.1700.10. 1 hit.
3.30.230.20. 1 hit.
HAMAPiMF_00388. LpxC. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4406.

Chemistry databases

BindingDBiP47205.
ChEMBLiCHEMBL3855.

Proteomic databases

PaxDbiP47205.
PRIDEiP47205.

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.
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. 1 hit.
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...

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: November 2, 2016
This is version 115 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.