ID A0A2D7NS92_9DELT Unreviewed; 387 AA. AC A0A2D7NS92; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 31-JUL-2019, entry version 10. DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523}; DE EC=2.3.1.- {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}; RN [1] {ECO:0000313|EMBL:MAJ49779.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED631 {ECO:0000313|EMBL:MAJ49779.1}; RX PubMed=29337314; DOI=10.1038/sdata.2017.203; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The reconstruction of 2,631 draft metagenome-assembled genomes from RT the global oceans."; RL Sci. Data 5:170203-170203(2018). CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine CC using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the CC biosynthesis of lipid A, a phosphorylated glycolipid that anchors CC the lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000256|HAMAP-Rule:MF_00523, ECO:0000256|SAAS:SAAS00760731}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-acyl-alpha-D- CC glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D- CC glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, CC ChEBI:CHEBI:137748; Evidence={ECO:0000256|HAMAP-Rule:MF_00523, CC ECO:0000256|SAAS:SAAS01123284}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00523, CC ECO:0000256|SAAS:SAAS00760697}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523, CC ECO:0000256|SAAS:SAAS00760705}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC LpxD subfamily. {ECO:0000256|HAMAP-Rule:MF_00523, CC ECO:0000256|SAAS:SAAS00760707}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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; PTHR43378; 1. DR Pfam; PF00132; Hexapep; 3. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523, KW ECO:0000256|SAAS:SAAS00760710, ECO:0000313|EMBL:MAJ49779.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00523, KW ECO:0000256|SAAS:SAAS00760688}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00523, KW ECO:0000256|SAAS:SAAS00760725}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00523, KW ECO:0000256|SAAS:SAAS00760733}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00523}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00523, KW ECO:0000256|SAAS:SAAS00760702, ECO:0000313|EMBL:MAJ49779.1}. FT REGION 1 32 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 363 383 {ECO:0000256|SAM:Coils}. FT COMPBIAS 1 20 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT ACT_SITE 287 287 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT 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 //