ID A0A0J1HA16_9GAMM Unreviewed; 339 AA.
AC A0A0J1HA16;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:KLV08509.1};
GN ORFNames=ABT56_03850 {ECO:0000313|EMBL:KLV08509.1};
OS Photobacterium aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1195763 {ECO:0000313|EMBL:KLV08509.1, ECO:0000313|Proteomes:UP000036097};
RN [1] {ECO:0000313|EMBL:KLV08509.1, ECO:0000313|Proteomes:UP000036097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12159 {ECO:0000313|EMBL:KLV08509.1,
RC ECO:0000313|Proteomes:UP000036097};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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:KLV08509.1}.
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DR EMBL; LDOT01000003; KLV08509.1; -; Genomic_DNA.
DR RefSeq; WP_047877551.1; NZ_LDOT01000003.1.
DR AlphaFoldDB; A0A0J1HA16; -.
DR STRING; 1195763.ABT56_03850; -.
DR PATRIC; fig|1195763.3.peg.823; -.
DR OrthoDB; 9784739at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000036097; 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; 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; 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:KLV08509.1};
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:KLV08509.1}.
FT DOMAIN 22..89
FT /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT acyltransferase non-repeat region"
FT /evidence="ECO:0000259|Pfam:PF04613"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 339 AA; 35555 MW; 4BE41C4D22D44006 CRC64;
MAGITLAEIA VKLDAELRGN GDVVIESVAA MGQAGEGQIT FLSNSKYRKQ LVDCAASAVM
LKADDADSFA GNVLIMNDPY LGFAKVAQLL DTTPAAAVDI APSAYIAEDA VIGEGVSVGH
NAVIESGARI GDHAQIGAGC FIGKDAVIGA RTKLWANVTI YHRVELGSDC LVQSSTVIGA
DGFGYANDKG EWVKIPQLGS VRIGNRVEIG ACTTIDRGAL EDTIIEDNVI IDNQMQIAHN
VQIGYGTAMA GGTIVAGSTK IGKYCIIGGA SVLNGHIEIA DGVTITGMGM VMRSIEEKGM
FSSGIPLQPN KEWRKTAARV MKIDEMNKRL KAVEKKLAD
//
