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LPXC_NOSS1
ID   LPXC_NOSS1              Reviewed;         280 AA.
AC   Q8YUR5;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=alr2270;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB73969.1; -; Genomic_DNA.
DR   PIR; AG2089; AG2089.
DR   RefSeq; WP_010996427.1; NZ_RSCN01000004.1.
DR   AlphaFoldDB; Q8YUR5; -.
DR   SMR; Q8YUR5; -.
DR   STRING; 103690.17131361; -.
DR   EnsemblBacteria; BAB73969; BAB73969; BAB73969.
DR   KEGG; ana:alr2270; -.
DR   eggNOG; COG0774; Bacteria.
DR   OMA; IVFYRSD; -.
DR   OrthoDB; 428602at2; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000002483; 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..280
FT                   /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT                   /id="PRO_0000191916"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   BINDING         77
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   280 AA;  30138 MW;  2174D1D12AB5DDA1 CRC64;
     MKQHTLAEAI AHTGVGLHSG VSTHVRILPA DAGSGRYFVR VDLPDSPTIP AQVAVVSQTV
     LSTQLGGGET GVRTVEHLLA ALAGMGVDNA RIEIDGPEIP LLDGSAQEWV TSIAEVGLVA
     QAVTNNLASF DIQEPIWIHQ DDAFVAAIPA SETRFSYGID FDLPAIGNQW YSWSLTTEPD
     TSFAQEIAPA RTFGLLHQIE YLQKSGLIKG GSLDNALICG PDGWVNPPLR FANEPVRHKI
     LDLVGDLSLL GYFPRAHFLA YKASHNLHIQ LAQRILALSN
 
 
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