ID Q9AI29_BURML Unreviewed; 305 AA. AC Q9AI29; Q62HH0; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 02-SEP-2026, entry version 140. DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00012745, ECO:0000256|HAMAP-Rule:MF_00388}; DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000256|HAMAP-Rule:MF_00388}; DE EC=3.5.1.108 {ECO:0000256|ARBA:ARBA00012745, ECO:0000256|HAMAP-Rule:MF_00388}; DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000256|HAMAP-Rule:MF_00388}; GN Name=wcbS {ECO:0000313|EMBL:AAK26475.1}; GN Synonyms=lpxC {ECO:0000256|HAMAP-Rule:MF_00388}; GN ORFNames=EGT70_13980 {ECO:0000313|EMBL:RPA24269.1}; OS Burkholderia mallei (Pseudomonas mallei). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=13373 {ECO:0000313|EMBL:AAK26475.1}; RN [1] {ECO:0000313|EMBL:AAK26475.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC23344 {ECO:0000313|EMBL:AAK26475.1}; RX PubMed=11373120; DOI=10.1006/mpat.2000.0430; RA DeShazer D., Waag D.M., Fritz D.L., Woods D.E.; RT "Identification of a Burkholderia mallei polysaccharide gene cluster by RT subtractive hybridization and demonstration that the encoded capsule is an RT essential virulence determinant."; RL Microb. Pathog. 30:253-269(2001). RN [2] {ECO:0000313|EMBL:RPA24269.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FDAARGOS_588 {ECO:0000313|EMBL:RPA24269.1}; RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Jaissle J., RA Tallon L.J., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A., RA Aluvathingal J., Nadendla S., Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_588; RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Jaissle J., RA Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A., Aluvathingal J., RA Nadendla S., Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (OCT-2018) 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:0000256|ARBA:ARBA00002923, CC ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00024535, ECO:0000256|HAMAP- CC Rule:MF_00388}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00005002, CC ECO:0000256|HAMAP-Rule:MF_00388}. CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000256|HAMAP- CC Rule:MF_00388}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF285636; AAK26475.1; -; Genomic_DNA. DR EMBL; RKJW01000002; RPA24269.1; -; Genomic_DNA. DR RefSeq; WP_004194036.1; NZ_AP029029.1. DR AlphaFoldDB; Q9AI29; -. DR GeneID; 92979980; -. DR KEGG; bmab:BM45_2454; -. DR KEGG; bmae:DM78_2658; -. DR KEGG; bmaf:DM51_1929; -. DR KEGG; bmai:DM57_1063; -. DR KEGG; bmal:DM55_1496; -. DR KEGG; bmaq:DM76_1474; -. DR PATRIC; fig|13373.22.peg.882; -. DR OMA; YHELWRA; -. DR UniPathway; UPA00359; UER00478. DR GO; GO:0103117; F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProtKB-ARBA. DR Gene3D; 3.30.230.20; lpxc deacetylase, domain 1; 1. DR Gene3D; 3.30.1700.10; lpxc deacetylase, domain 2; 1. DR HAMAP; MF_00388; LpxC; 1. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. 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 NCBIfam; NF009666; PRK13187.1; 1. DR PANTHER; PTHR33694; UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED; 1. DR PANTHER; PTHR33694:SF1; UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF03331; LpxC; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00388}; KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00388}. FT ACT_SITE 280 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" FT BINDING 253 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" FT BINDING 257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" SQ SEQUENCE 305 AA; 33143 MW; EED7108512266A71 CRC64; MSVPTGWATS QGTLARALTI DGHGLHTGRR VGVRILPARP EDGVTGIAFR RVEQGRTLAT LPVDPALRRA QPLCTMLRNA DGVGVRTVEH LLASLLACEI DHAIVELDAE EVPILDGSAT PWVDAIRTCG RVALDAPKRF IRVLRTVVVT EGEGEQRREM RIEPAPRYEL SVRNDLRGFG EMHWDGALTP AAFATEIAPS RSYGRVKWAV PAILAGYLRG MPILRGARPS CTASIVGKRV LGGMRLPDEF VRHRVLDLVG DLALAGAPLL ARVSAVRPGH EMNFRLVDAL LAEPGAWQWA DFSEA //