ID LPXD_ACIBS Reviewed; 356 AA. AC B0VMV2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523}; DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523}; GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; GN OrderedLocusNames=ABSDF1688; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3- CC hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of CC lipid A, a phosphorylated glycolipid that anchors the CC lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]- CC alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D- CC glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA- CC COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748; CC EC=2.3.1.191; Evidence={ECO:0000255|HAMAP-Rule:MF_00523}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}. 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; CU468230; CAP01028.1; -; Genomic_DNA. DR PDB; 4E75; X-ray; 2.85 A; A/B/C/D/E/F=2-355. DR PDB; 4E79; X-ray; 2.66 A; A/B/C=2-355. DR PDBsum; 4E75; -. DR PDBsum; 4E79; -. DR AlphaFoldDB; B0VMV2; -. DR SMR; B0VMV2; -. DR KEGG; abm:ABSDF1688; -. DR HOGENOM; CLU_049865_0_1_6; -. DR BRENDA; 2.3.1.191; 98. DR UniPathway; UPA00973; -. DR Proteomes; UP000001741; Chromosome. DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03352; LbH_LpxD; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1. DR HAMAP; MF_00523; LpxD; 1. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR007691; LpxD. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep. DR NCBIfam; TIGR01853; lipid_A_lpxD; 1. DR PANTHER; PTHR43378; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE; 1. DR PANTHER; PTHR43378:SF2; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00132; Hexapep; 2. DR Pfam; PF04613; LpxD; 1. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Repeat; Transferase. FT CHAIN 1..356 FT /note="UDP-3-O-acylglucosamine N-acyltransferase" FT /id="PRO_1000127656" FT ACT_SITE 242 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523" FT HELIX 8..14 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 18..21 FT /evidence="ECO:0007829|PDB:4E79" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:4E79" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:4E79" FT HELIX 50..55 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 59..63 FT /evidence="ECO:0007829|PDB:4E79" FT HELIX 65..69 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:4E79" FT HELIX 83..91 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:4E79" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:4E79" FT HELIX 313..326 FT /evidence="ECO:0007829|PDB:4E79" FT HELIX 333..346 FT /evidence="ECO:0007829|PDB:4E79" SQ SEQUENCE 356 AA; 38484 MW; BF15F948205840F6 CRC64; MKVQQYRLDE LAHLVKGELI GEGSLQFSNL ASLENAEVNH LTFVNGEKHL DQAKVSRAGA YIVTAALKEH LPEKDNFIIV DNPYLAFAIL THVFDKKISS TGIESTARIH PSAVISETAY IGHYVVIGEN CVVGDNTVIQ SHTKLDDNVE VGKDCFIDSY VTITGSSKLR DRVRIHSSTV IGGEGFGFAP YQGKWHRIAQ LGSVLIGNDV RIGSNCSIDR GALDNTILED GVIIDNLVQI AHNVHIGSNT AIAAKCGIAG STKIGKNCIL AGACGVAGHL SIADNVTLTG MSMVTKNISE AGTYSSGTGL FENNHWKKTI VRLRQLADVP LTQITKRLDH IQAQIESLES TFNLRK //