ID A0A2D7NS92_9DELT Unreviewed; 387 AA. AC A0A2D7NS92; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 14-DEC-2022, entry version 17. DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523}; DE EC=2.3.1.191 {ECO:0000256|HAMAP-Rule:MF_00523}; GN Name=lpxD {ECO:0000256|HAMAP-Rule:MF_00523, GN ECO:0000313|EMBL:MAJ49779.1}; GN ORFNames=CL937_08770 {ECO:0000313|EMBL:MAJ49779.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ49779.1, ECO:0000313|Proteomes:UP000226880}; RN [1] {ECO:0000313|Proteomes:UP000226880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_00523}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00523}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00523}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MAJ49779.1}. 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; NZHX01000138; MAJ49779.1; -; Genomic_DNA. DR UniPathway; UPA00973; -. DR Proteomes; UP000226880; Unassembled WGS sequence. 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 HAMAP; MF_00523; LpxD; 1. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR007691; LpxD. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR PANTHER; PTHR43378; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE; 1. DR Pfam; PF00132; Hexapep; 3. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1. DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523, KW ECO:0000313|EMBL:MAJ49779.1}; KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP- KW Rule:MF_00523}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_00523}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_00523}; Repeat {ECO:0000256|HAMAP-Rule:MF_00523}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00523, ECO:0000313|EMBL:MAJ49779.1}. FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 287 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523" SQ SEQUENCE 387 AA; 41108 MW; C3054595A27354D7 CRC64; MDRSSFSCNA RRNPGQGQAP GQRNRDGAFL KNQKPGLTLE ELAAKLGAEF QGQADLKLTC SCGLDSLQKG GLAYVTGSGG IGNVPVPAEL DRSLRKAPEE NVGKETALIV PLNYEPRTGN LIFAEDPLDM HVKATRLLHP PLIPASGTHP SAIIADDAEL AVGVSVGPNT VIGNGVKIGE RSRIHAGVVI LDQASIGNDC EIFPNAVIQD RCLIGNRVII QSNAVIGADG HGYYQREGIN LKIPQIGIVV LEDDVEIGAG TTIDRARFTR TVIGRGSKID NXVQVAHNVT IGEQALISAQ TAIGGSAQAG DHLILGGQTG VRDNVRVGSN VTLAARGVIT ANTKDHELLG GMPSRPLSEW RKIQSLINRL GELFERVRKL EQKKDQP //