ID LPXA_PARP8 Reviewed; 262 AA. AC B2JIB4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 92. DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387}; GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387}; GN OrderedLocusNames=Bphy_1326; OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / OS STM815) (Burkholderia phymatum). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=391038; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815; RX PubMed=25197461; DOI=10.4056/sigs.4861021; RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R., RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D., RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M., RA Bristow J., Riley M.; RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host RT range and efficient nitrogen-fixing symbiont of Mimosa species."; RL Stand. Genomic Sci. 9:763-774(2014). CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated CC glycolipid that anchors the lipopolysaccharide to the outer membrane of CC the cell. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo- CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA- CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827, CC ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00387}; 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 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00387}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}. 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; CP001043; ACC70508.1; -; Genomic_DNA. DR RefSeq; WP_012400722.1; NC_010622.1. DR AlphaFoldDB; B2JIB4; -. DR SMR; B2JIB4; -. DR STRING; 391038.Bphy_1326; -. DR KEGG; bph:Bphy_1326; -. DR eggNOG; COG1043; Bacteria. DR HOGENOM; CLU_061249_0_0_4; -. DR OrthoDB; 9807278at2; -. DR UniPathway; UPA00359; UER00477. DR Proteomes; UP000001192; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03351; LbH_UDP-GlcNAc_AT; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 1. DR HAMAP; MF_00387; LpxA; 1. DR InterPro; IPR029098; Acetyltransf_C. DR InterPro; IPR037157; Acetyltransf_C_sf. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR010137; Lipid_A_LpxA. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR NCBIfam; TIGR01852; lipid_A_lpxA; 1. DR NCBIfam; NF003657; PRK05289.1; 1. DR PANTHER; PTHR43480; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE; 1. DR PANTHER; PTHR43480:SF1; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF13720; Acetyltransf_11; 1. DR Pfam; PF00132; Hexapep; 2. DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Reference proteome; Repeat; Transferase. FT CHAIN 1..262 FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine FT O-acyltransferase" FT /id="PRO_1000122691" SQ SEQUENCE 262 AA; 27846 MW; 1DE2905EEE198037 CRC64; MSRIHPTAII ESGAQLDESV EIGPYAIVGA NVTIGARTTI GSHSVIEGHT TIGEDNRIGH YASVGGRPQD MKYRDEPTKL VIGSRNTIRE FTTIHTGTVQ DKGITTLGDD NWIMAYVHIG HDCQIGSNVI LSSNAQMAGH VIVGDHAIVG GMSGVHQFVR IGAHSMLGGA SALVQDIPPF VIAAGNKAEP HGINVEGLRR RGFSADAISA LRSAYRLLYK NGLSLEDAKV QLRELAAAGG DGDEPVRALV DFVEQSQRGI IR //