LPXC_PSEAB
ID LPXC_PSEAB Reviewed; 303 AA.
AC Q02H34;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=PA14_57260;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ13677.1; -; Genomic_DNA.
DR RefSeq; WP_003141270.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02H34; -.
DR SMR; Q02H34; -.
DR PRIDE; Q02H34; -.
DR EnsemblBacteria; ABJ13677; ABJ13677; PA14_57260.
DR KEGG; pau:PA14_57260; -.
DR HOGENOM; CLU_046528_1_0_6; -.
DR OMA; IVFYRSD; -.
DR BioCyc; PAER208963:G1G74-4823-MON; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000000653; 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_1000013218"
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; 33467 MW; A41408C1A6CC9C22 CRC64;
MIKQRTLKNI IRATGVGLHS GEKVYLTLKP APMDTGIVFC RTDLDPVVEI PARAENVGET
TMSTTLVKGD VKVDTVEHLL SAMAGLGIDN AYVELSASEV PIMDGSAGPF VFLIQSAGLQ
EQEAAKKFIR IKREVSVEEG DKRAVFVPFD GFKVSFEIDF DHPVFRGRTQ QASVDFSSTS
FVKEVSRART FGFMRDIEYL RSQNLALGGS VENAIVVDEN RVLNEDGLRY EDEFVKHKIL
DAIGDLYLLG NSLIGEFRGF KSGHALNNQL LRTLIADKDA WEVVTFEDAR TAPISYMRPA
AAV
