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LPXC_RICB8
ID   LPXC_RICB8              Reviewed;         288 AA.
AC   A8GWA4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=A1I_03890;
OS   Rickettsia bellii (strain OSU 85-389).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=391896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-389;
RA   Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT   "Complete genome sequencing of Rickettsia bellii.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000849; ABV79131.1; -; Genomic_DNA.
DR   RefSeq; WP_011477616.1; NC_009883.1.
DR   AlphaFoldDB; A8GWA4; -.
DR   SMR; A8GWA4; -.
DR   KEGG; rbo:A1I_03890; -.
DR   HOGENOM; CLU_046528_1_1_5; -.
DR   OMA; IVFYRSD; -.
DR   UniPathway; UPA00359; UER00478.
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..288
FT                   /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT                   /id="PRO_1000013223"
FT   ACT_SITE        263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ   SEQUENCE   288 AA;  31987 MW;  522E08514A79DB28 CRC64;
     MQQITLSKPV SCYGIGVHSG KRTQLTIEPA KENTGIIFIR TDISSENNYI EAKYFNVSDT
     LLSTTISNSN KIQVSTIEHI MAALWGCGID NAVIKIDGPE VPIMDGSSKP FVFMIECAGK
     KLQNAPKKYL KILKEVTATH KDCELTCTPS DHMKIDLTID FNSKAIGRQN LVFSKQESFN
     NNIADARTFG FTKDGDYLQS KGLALGVSFE NTIAIDDQDK VLNPDGLRYQ DEFVRHKLLD
     LFGDLYTSGN NIVSSINGYK TSHALNNELL QRIFSDNTSH KFVTASEI
 
 
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