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LPXC_SHELP
ID   LPXC_SHELP              Reviewed;         306 AA.
AC   A3QIL6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Shew_3448;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-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; CP000606; ABO25314.1; -; Genomic_DNA.
DR   RefSeq; WP_011867244.1; NC_009092.1.
DR   AlphaFoldDB; A3QIL6; -.
DR   SMR; A3QIL6; -.
DR   STRING; 323850.Shew_3448; -.
DR   EnsemblBacteria; ABO25314; ABO25314; Shew_3448.
DR   KEGG; slo:Shew_3448; -.
DR   eggNOG; COG0774; Bacteria.
DR   HOGENOM; CLU_046528_1_0_6; -.
DR   OMA; IVFYRSD; -.
DR   OrthoDB; 428602at2; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000001558; 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; Reference proteome; Zinc.
FT   CHAIN           1..306
FT                   /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT                   /id="PRO_1000013230"
FT   ACT_SITE        265
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         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ   SEQUENCE   306 AA;  33803 MW;  3F86571759529216 CRC64;
     MIFQRTVKEM VKTTGVGLHS GNKVTLTIKP APVNTGIVLV RTDLTPSVAI AAKADQVRET
     TMCTALVNDE GVRISTIEHL FAALAGLGID NATIEVDAPE IPIMDGSASP WVFLLQSVGI
     QEQSAAKKYL RIKRPVRVED GDKWAELRPF KGFRVDFAID FNHPEIARSQ QHMVMDFSSS
     AFVRDISRAR TFGFMRDIEY LRANNLALGG SMENAVVLDE YRVLNPDGLR YEDEFVKHKI
     LDAFGDLYVA GHAIVGEFRA FKTGHALNNQ LVRALLAEQD AWELVSFEKE EEVPVSFAVP
     AGAVLA
 
 
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