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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications
Metal bindingi226 – 2261Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications
Metal bindingi230 – 2301ZincUniRule annotationCombined sources2 Publications
Active sitei253 – 2531Proton donorUniRule annotation1 Publication

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

BioCyciAAEO224324:GJBH-1269-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191H → A: 20-fold decrease in activity. 2-fold decrease in zinc content. 1 Publication
Mutagenesisi19 – 191H → Q: 2-fold decrease in activity. 1 Publication
Mutagenesisi19 – 191H → Y: 22-fold decrease in activity. 1 Publication
Mutagenesisi73 – 731E → A: 10-fold decrease in activity. 3.6-fold decrease in zinc content. 1 Publication
Mutagenesisi73 – 731E → Q: Loss of activity. 1 Publication
Mutagenesisi74 – 741H → A: Almost loss of activity. 10-fold decrease in zinc content. 1 Publication
Mutagenesisi74 – 741H → Q: Almost loss of activity. 1 Publication
Mutagenesisi95 – 951E → A, N or S: Almost no change in activity. 1 Publication
Mutagenesisi100 – 1001D → A, N or S: Almost no change in activity. 1 Publication
Mutagenesisi222 – 2221E → A: 20-fold decrease in activity. 1 Publication
Mutagenesisi222 – 2221E → N: Loss of activity. 1 Publication
Mutagenesisi222 – 2221E → S: 15-fold decrease in activity. 1 Publication
Mutagenesisi226 – 2261H → A: 720-fold decrease in activity. 16.6-fold decrease in zinc content. 1 Publication
Mutagenesisi234 – 2341D → A: Almost loss of activity. 1.5-fold decrease in zinc content. 1 Publication
Mutagenesisi234 – 2341D → N: 29-fold decrease in activity. 1 Publication
Mutagenesisi234 – 2341D → S: Loss of activity. 1 Publication
Mutagenesisi253 – 2531H → A: Loss of activity. 4.3-fold decrease in zinc content. 1 Publication
Mutagenesisi253 – 2531H → Q: Loss of activity. 1 Publication

Chemistry

ChEMBLiCHEMBL1075040.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282UDP-3-O-acyl-N-acetylglucosamine deacetylasePRO_0000191917Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_1772.

Chemistry

BindingDBiO67648.

Structurei

Secondary structure

1
282
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 – 308Combined sources
Beta strandi37 – 415Combined sources
Beta strandi44 – 496Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 644Combined sources
Beta strandi67 – 704Combined sources
Helixi73 – 8210Combined sources
Beta strandi86 – 9510Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 1118Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi148 – 1547Combined sources
Beta strandi161 – 1677Combined sources
Helixi171 – 1733Combined sources
Turni174 – 1763Combined sources
Beta strandi180 – 1823Combined sources
Helixi183 – 1919Combined sources
Turni200 – 2023Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi211 – 2133Combined sources
Helixi222 – 23514Combined sources
Helixi236 – 2383Combined sources
Beta strandi245 – 2506Combined sources
Helixi253 – 27119Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-270.
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
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. Positions 3-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1772.

Chemistry

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.
BioCyciAAEO224324:GJBH-1269-MONOMER.
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: September 7, 2016
This is version 117 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.