ID A0A448VM70_9NEIS Unreviewed; 353 AA.
AC A0A448VM70;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:VEJ50866.1};
GN ORFNames=NCTC12742_00913 {ECO:0000313|EMBL:VEJ50866.1};
OS Neisseria weaveri.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=28091 {ECO:0000313|EMBL:VEJ50866.1, ECO:0000313|Proteomes:UP000272771};
RN [1] {ECO:0000313|EMBL:VEJ50866.1, ECO:0000313|Proteomes:UP000272771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12742 {ECO:0000313|EMBL:VEJ50866.1,
RC ECO:0000313|Proteomes:UP000272771};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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}.
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DR EMBL; LR134533; VEJ50866.1; -; Genomic_DNA.
DR RefSeq; WP_004283149.1; NZ_POXU01000008.1.
DR AlphaFoldDB; A0A448VM70; -.
DR STRING; 28091.SAMEA3174300_01537; -.
DR KEGG; nwe:SAMEA3174300_1537; -.
DR OrthoDB; 9784739at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000272771; Chromosome 1.
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; IPR018357; Hexapep_transf_CS.
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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00523}; Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000272771};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00523}.
FT DOMAIN 25..93
FT /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT acyltransferase non-repeat region"
FT /evidence="ECO:0000259|Pfam:PF04613"
FT COILED 321..348
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 353 AA; 36974 MW; C949CC699ACCBB00 CRC64;
MKTNNQIYTL SQIVGKLGGE QRGADIAVEA VKPLAEAKEN HISFLANPKY TAEVKESLAG
IVIVSAKVAD DFAGRSLIIA PDPYLYFAKV ARLFSPIVEP APGIHPTAVI EEGAVVPDSC
EIGAHVYIGA DTVLGEGCRI LAGAVIEHGC KLGDGVFMHP KAVVYHGCTL GNRVEIHSGA
VIGADGFGLA FAGDSWFKIP QTGGVTLGDD VEIGSNSNID RGAMSDTVVG NGTKIDNQVQ
IGHNCKIGSH TVIAAKTGIS GSVTIGNYCI IGGGVGTVGH IEIADKTTIG GGSSITHSIK
ESGQHIAGPY PMQTHKEWAR NAVHIRHLSE MNKRIKQLEK ALETSQSADN NKE
//
