ID D1W5C3_9BACT Unreviewed; 345 AA.
AC D1W5C3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:EFA92324.1};
GN ORFNames=HMPREF0650_0788 {ECO:0000313|EMBL:EFA92324.1};
OS Hoylesella buccalis ATCC 35310.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=679190 {ECO:0000313|EMBL:EFA92324.1, ECO:0000313|Proteomes:UP000005283};
RN [1] {ECO:0000313|EMBL:EFA92324.1, ECO:0000313|Proteomes:UP000005283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35310 {ECO:0000313|EMBL:EFA92324.1,
RC ECO:0000313|Proteomes:UP000005283};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Prevotella buccalis ATCC 35310.";
RL Submitted (DEC-2009) 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:EFA92324.1}.
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DR EMBL; ADEG01000045; EFA92324.1; -; Genomic_DNA.
DR RefSeq; WP_004348906.1; NZ_ADEG01000045.1.
DR AlphaFoldDB; D1W5C3; -.
DR STRING; 679190.HMPREF0650_0788; -.
DR eggNOG; COG1044; Bacteria.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000005283; 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 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW ECO:0000313|EMBL:EFA92324.1};
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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00523};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00523, ECO:0000313|EMBL:EFA92324.1}.
FT DOMAIN 21..90
FT /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT acyltransferase non-repeat region"
FT /evidence="ECO:0000259|Pfam:PF04613"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 345 AA; 37557 MW; B88DC574548EA887 CRC64;
MEFTAKQIAQ YIGGKIEGNE DATVHTFAKI EEGTNGAISF LSNPKYTHYI YNTQSSIVLI
DEDLKLDKPV QTTLIRVKNA YDSVAKLLQL YESTKPRKTG IHPMANIAKT AKIGENAYIG
PFAYIGENVV IGNNTQIFPH AVVLENASVG SECIIYPHAT VYHNCKIGNR VILHAGSVIG
ADGFGFAPSK DGYDKIPQIG IVTIEDDVEV GANTCVDRST MGSTYVRKGV KLDNLVQIAH
NTDIGEHTVM SAQVGVAGSS KVGQWCMFGG QVGVAGHITI GNKVFLGAQS GVPGSIKDNQ
QLIGTPPMKE RAYFRSQAIF RKLPELYKEI NNLKEEVERL KKNIK
//
