LPXD_ACISJ
ID LPXD_ACISJ Reviewed; 326 AA.
AC A1W908;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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}; OrderedLocusNames=Ajs_2575;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) 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: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}.
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DR EMBL; CP000539; ABM42733.1; -; Genomic_DNA.
DR RefSeq; WP_011805770.1; NC_008782.1.
DR AlphaFoldDB; A1W908; -.
DR SMR; A1W908; -.
DR STRING; 232721.Ajs_2575; -.
DR EnsemblBacteria; ABM42733; ABM42733; Ajs_2575.
DR KEGG; ajs:Ajs_2575; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_0_4; -.
DR OMA; QIQIAHN; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000645; 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 HAMAP; MF_00523; LpxD; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR007691; LpxD.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR PANTHER; PTHR43378; PTHR43378; 1.
DR Pfam; PF00132; Hexapep; 2.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..326
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_1000050921"
FT ACT_SITE 225
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 326 AA; 34504 MW; E76038C0B534FF39 CRC64;
MSLRLGQIVD ALGGSLEGGE RDTEILRIAP LESSGPGDLS FLSNPRYQSQ LAASQAACVI
VAPAMRNAAL ERGACIVVEQ PYTYFAHVTQ LWVRAHGQGA PAGIHPSAVV DPQARVAPTA
SIGPLCVVER GAVIGAHTVL KSRVTVGERC TVGERCILHP GVVIGADGFG FAQQRGEWIK
IEQLGAVRIG NDVEIGANTC IDRGALDDTV IEDGVKLDNL IQIAHNVHIG RHTAMAGCSA
VAGSTRIGAH CTIAGAASIV GHLQLADNVH ISTNTVVTHS ITQPGQYTGV FPMDDNAKWE
KNAATLRQLY RLRERIKALE QTRKDG