ID LPXC_BURCJ Reviewed; 305 AA. AC B4E5Y5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 11-DEC-2019, entry version 63. 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}; GN OrderedLocusNames=BceJ2315_33930; ORFNames=BCAL3455; OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=216591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610; RX PubMed=18931103; DOI=10.1128/jb.01230-08; RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D., RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S., RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K., RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D., RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R., RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.; RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of RT cystic fibrosis patients."; RL J. Bacteriol. 191:261-277(2009). 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=H2O + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D- CC glucosamine = acetate + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha- CC D-glucosamine; Xref=Rhea:RHEA:25209, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:61494, ChEBI:CHEBI:71573; CC EC=3.5.1.108; 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}. 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; AM747720; CAR53778.1; -; Genomic_DNA. DR RefSeq; WP_006487145.1; NC_011000.1. DR SMR; B4E5Y5; -. DR STRING; 216591.BCAL3455; -. DR EnsemblBacteria; CAR53778; CAR53778; BCAL3455. DR KEGG; bcj:BCAL3455; -. DR eggNOG; ENOG4105C7C; Bacteria. DR eggNOG; COG0774; LUCA. DR HOGENOM; HOG000256663; -. DR KO; K02535; -. DR OMA; IVFYRSD; -. DR OrthoDB; 428602at2; -. DR BioCyc; BCEN216591:G1G1V-3842-MONOMER; -. DR UniPathway; UPA00359; UER00478. DR Proteomes; UP000001035; Chromosome 1. 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..305 FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase" FT /id="PRO_1000122767" FT ACT_SITE 264 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388" FT METAL 78 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388" FT METAL 237 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388" FT METAL 241 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388" SQ SEQUENCE 305 AA; 33506 MW; B50FCEB0DA411055 CRC64; MLKQRTIKSI VKTVGIGVHS GRKIELTLRP AAPGTGIVFS RVDLPTPVDI PASAMSIGDT RLASVLQKDG VRVSTVEHLM SACAGLGIDN LYVDVTAEEI PIMDGSAATF VFLIQSAGIE EQNAPKRFIK VKKPVEIRDG DKFARLDPYF GFKLKFSIDF RHPAVDKTGQ ELEVDFATTS YVREIARART FGFAHEAEML REIGLARGGS MDNAIVLDEY RILNNDGLRY DDEFVKHKML DAIGDLYVIG HPLLASYTAY KSGHGLNNAL LRELLAHEDA YEIVTFDDPQ AAPKGFAFDA QTAFA //