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Protein

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

Gene

lpxC

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation2 Publications

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. no protein annotated in this organism
  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 bindingi74Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications1
Metal bindingi226Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications1
Metal bindingi230ZincUniRule annotationCombined sources2 Publications1
Active sitei253Proton donorUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

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. 396.
UniPathwayiUPA00359; UER00478.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-3-O-acyl-N-acetylglucosamine deacetylaseUniRule annotation (EC:3.5.1.108UniRule annotation2 Publications)
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:aq_1772
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19H → A: 20-fold decrease in activity. 2-fold decrease in zinc content. 1 Publication1
Mutagenesisi19H → Q: 2-fold decrease in activity. 1 Publication1
Mutagenesisi19H → Y: 22-fold decrease in activity. 1 Publication1
Mutagenesisi73E → A: 10-fold decrease in activity. 3.6-fold decrease in zinc content. 1 Publication1
Mutagenesisi73E → Q: Loss of activity. 1 Publication1
Mutagenesisi74H → A: Almost loss of activity. 10-fold decrease in zinc content. 1 Publication1
Mutagenesisi74H → Q: Almost loss of activity. 1 Publication1
Mutagenesisi95E → A, N or S: Almost no change in activity. 1 Publication1
Mutagenesisi100D → A, N or S: Almost no change in activity. 1 Publication1
Mutagenesisi222E → A: 20-fold decrease in activity. 1 Publication1
Mutagenesisi222E → N: Loss of activity. 1 Publication1
Mutagenesisi222E → S: 15-fold decrease in activity. 1 Publication1
Mutagenesisi226H → A: 720-fold decrease in activity. 16.6-fold decrease in zinc content. 1 Publication1
Mutagenesisi234D → A: Almost loss of activity. 1.5-fold decrease in zinc content. 1 Publication1
Mutagenesisi234D → N: 29-fold decrease in activity. 1 Publication1
Mutagenesisi234D → S: Loss of activity. 1 Publication1
Mutagenesisi253H → A: Loss of activity. 4.3-fold decrease in zinc content. 1 Publication1
Mutagenesisi253H → Q: Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075040.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001919171 – 282UDP-3-O-acyl-N-acetylglucosamine deacetylaseAdd BLAST282

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_1772.

Chemistry databases

BindingDBiO67648.

Structurei

Secondary structure

1282
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 – 30Combined sources8
Beta strandi37 – 41Combined sources5
Beta strandi44 – 49Combined sources6
Helixi50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi61 – 64Combined sources4
Beta strandi67 – 70Combined sources4
Helixi73 – 82Combined sources10
Beta strandi86 – 95Combined sources10
Beta strandi101 – 103Combined sources3
Helixi104 – 111Combined sources8
Beta strandi114 – 120Combined sources7
Beta strandi130 – 134Combined sources5
Beta strandi137 – 142Combined sources6
Beta strandi148 – 154Combined sources7
Beta strandi161 – 167Combined sources7
Helixi171 – 173Combined sources3
Turni174 – 176Combined sources3
Beta strandi180 – 182Combined sources3
Helixi183 – 191Combined sources9
Turni200 – 202Combined sources3
Beta strandi204 – 206Combined sources3
Beta strandi211 – 213Combined sources3
Helixi222 – 235Combined sources14
Helixi236 – 238Combined sources3
Beta strandi245 – 250Combined sources6
Helixi253 – 271Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P42X-ray2.00A/B2-271[»]
1XXENMR-A1-282[»]
1YH8X-ray2.70A/B2-271[»]
1YHCX-ray2.10A/B2-271[»]
2GO3X-ray2.00A/B1-255[»]
2GO4X-ray2.70A/B1-267[»]
2IERX-ray2.70A/B1-271[»]
2IESX-ray3.10A/B1-271[»]
2J65X-ray2.20A/B1-271[»]
2JT2NMR-A1-274[»]
2O3ZX-ray2.25A/B1-271[»]
3P3CX-ray1.25A2-275[»]
3P76X-ray1.93A1-271[»]
4OZEX-ray1.61A/B1-282[»]
4U3BX-ray1.34A1-271[»]
4U3DX-ray1.25A1-271[»]
5DROX-ray2.01A/B1-274[»]
5DRPX-ray1.89A/B1-274[»]
ProteinModelPortaliO67648.
SMRiO67648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67648.

Family & Domainsi

Sequence similaritiesi

Belongs to the LpxC family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C7C. Bacteria.
COG0774. LUCA.
HOGENOMiHOG000256664.
InParanoidiO67648.
KOiK02535.
OMAiDGSAIQW.
OrthoDBiPOG091H0292.

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.

O67648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLEKTVKEK LSFEGVGIHT GEYSKLIIHP EKEGTGIRFF KNGVYIPARH
60 70 80 90 100
EFVVHTNHST DLGFKGQRIK TVEHILSVLH LLEITNVTIE VIGNEIPILD
110 120 130 140 150
GSGWEFYEAI RKNILNQNRE IDYFVVEEPI IVEDEGRLIK AEPSDTLEVT
160 170 180 190 200
YEGEFKNFLG RQKFTFVEGN EEEIVLARTF CFDWEIEHIK KVGLGKGGSL
210 220 230 240 250
KNTLVLGKDK VYNPEGLRYE NEPVRHKVFD LIGDLYLLGS PVKGKFYSFR
260 270 280
GGHSLNVKLV KELAKKQKLT RDLPHLPSVQ AL
Length:282
Mass (Da):32,145
Last modified:August 1, 1998 - v1
Checksum:i38EFE076144B5F27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07605.1.
PIRiF70452.
RefSeqiNP_214214.1. NC_000918.1.
WP_010881151.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07605; AAC07605; aq_1772.
GeneIDi1193363.
KEGGiaae:aq_1772.
PATRICi20960534. VBIAquAeo85532_1368.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07605.1.
PIRiF70452.
RefSeqiNP_214214.1. NC_000918.1.
WP_010881151.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P42X-ray2.00A/B2-271[»]
1XXENMR-A1-282[»]
1YH8X-ray2.70A/B2-271[»]
1YHCX-ray2.10A/B2-271[»]
2GO3X-ray2.00A/B1-255[»]
2GO4X-ray2.70A/B1-267[»]
2IERX-ray2.70A/B1-271[»]
2IESX-ray3.10A/B1-271[»]
2J65X-ray2.20A/B1-271[»]
2JT2NMR-A1-274[»]
2O3ZX-ray2.25A/B1-271[»]
3P3CX-ray1.25A2-275[»]
3P76X-ray1.93A1-271[»]
4OZEX-ray1.61A/B1-282[»]
4U3BX-ray1.34A1-271[»]
4U3DX-ray1.25A1-271[»]
5DROX-ray2.01A/B1-274[»]
5DRPX-ray1.89A/B1-274[»]
ProteinModelPortaliO67648.
SMRiO67648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1772.

Chemistry databases

BindingDBiO67648.
ChEMBLiCHEMBL1075040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07605; AAC07605; aq_1772.
GeneIDi1193363.
KEGGiaae:aq_1772.
PATRICi20960534. VBIAquAeo85532_1368.

Phylogenomic databases

eggNOGiENOG4105C7C. Bacteria.
COG0774. LUCA.
HOGENOMiHOG000256664.
InParanoidiO67648.
KOiK02535.
OMAiDGSAIQW.
OrthoDBiPOG091H0292.

Enzyme and pathway databases

UniPathwayiUPA00359; UER00478.
BRENDAi3.5.1.108. 396.

Miscellaneous databases

EvolutionaryTraceiO67648.

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_AQUAE
AccessioniPrimary (citable) accession number: O67648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 119 of the entry and version 1 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.