LPXC_PSEPF
ID LPXC_PSEPF Reviewed; 303 AA.
AC Q3K750;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
DE EC=3.5.1.108 {ECO:0000255|HAMAP-Rule:MF_00388};
DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
GN Name=lpxC {ECO:0000255|HAMAP-Rule:MF_00388}; OrderedLocusNames=Pfl01_4667;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-
CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the
CC committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine +
CC H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate;
CC Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP-
CC Rule:MF_00388}.
CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000255|HAMAP-
CC Rule:MF_00388}.
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DR EMBL; CP000094; ABA76404.1; -; Genomic_DNA.
DR RefSeq; WP_007956752.1; NC_007492.2.
DR AlphaFoldDB; Q3K750; -.
DR SMR; Q3K750; -.
DR STRING; 205922.Pfl01_4667; -.
DR PRIDE; Q3K750; -.
DR EnsemblBacteria; ABA76404; ABA76404; Pfl01_4667.
DR KEGG; pfo:Pfl01_4667; -.
DR eggNOG; COG0774; Bacteria.
DR HOGENOM; CLU_046528_1_0_6; -.
DR OMA; IVFYRSD; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000002704; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0103117; F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1700.10; -; 1.
DR Gene3D; 3.30.230.20; -; 1.
DR HAMAP; MF_00388; LpxC; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR004463; UDP-acyl_GlcNac_deAcase.
DR InterPro; IPR011334; UDP-acyl_GlcNac_deAcase_C.
DR InterPro; IPR015870; UDP-acyl_N-AcGlcN_deAcase_N.
DR PANTHER; PTHR33694; PTHR33694; 1.
DR Pfam; PF03331; LpxC; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR TIGRFAMs; TIGR00325; lpxC; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Zinc.
FT CHAIN 1..303
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT /id="PRO_0000253684"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ SEQUENCE 303 AA; 33245 MW; 46795F6C4ADC1144 CRC64;
MIKQRTLKNI IRATGVGLHS GEKVYLTLKP APVDTGIVFR RADLDPVVEI PARAANVGET
TMSTTLVNGD VKVDTVEHLL SAMAGLGIDN AYVELSASEV PIMDGSAGPF VFLIQSAGLE
EQDAAKKFIR ILREVTVEDG DKRATFVPFE GFKVSFEIDF DHPVFRDRTQ SASVDFSSTS
FVKEVSRART FGFMSDIEYL RKHNLALGGS VENAIVVDAD GVLNEDGLRY EDEFVKHKIL
DAIGDLYLLG NSLIGEFKGF KSGHALNNQL LRKLIEQKDA WEVVTFEDAS TAPISYMRPV
AAV
