ID A0A086AMV4_9FLAO Unreviewed; 343 AA.
AC A0A086AMV4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=IW22_18710 {ECO:0000313|EMBL:KFF18018.1};
OS Chryseobacterium sp. JM1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1233950 {ECO:0000313|EMBL:KFF18018.1, ECO:0000313|Proteomes:UP000028731};
RN [1] {ECO:0000313|EMBL:KFF18018.1, ECO:0000313|Proteomes:UP000028731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM1 {ECO:0000313|EMBL:KFF18018.1,
RC ECO:0000313|Proteomes:UP000028731};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Chryseobacterium sp. JM1.";
RL Submitted (JUL-2014) 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:KFF18018.1}.
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DR EMBL; JPRN01000012; KFF18018.1; -; Genomic_DNA.
DR RefSeq; WP_034729171.1; NZ_JPRN01000012.1.
DR AlphaFoldDB; A0A086AMV4; -.
DR eggNOG; COG1044; Bacteria.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000028731; 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; 3.
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:KFF18018.1};
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:KFF18018.1}.
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 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 343 AA; 37136 MW; AC1113FD2341D6A7 CRC64;
MEFTASQIAS FIDGQIIGDE STVITGVSPI ENGESGHLSF IAQDRFSHFL DTSKCSVIIV
SEKLIDKVNY NPTLIVVKDA YLSFQILMNL YQEMQGRKEG IETGSSIHET AVIGDKAYIG
AFTYVSEKAK IGEGAQIYPH VYIGKGVKIG KNCKIDSGAR IYDYCIIGDN CVIHSNTVVG
GDGFGFQPTA EGFKKIPQLG NVIIEDDVEI GSNCSIDRAT IGSTIIGKGT KIDNLIQIAH
NVKIGQNNVI AAQAGIAGST TIGDWNQIGG QVGVVGHIKI GNQVKIQAQS GVNSSVNDKE
TLYGSPAISY NDYLRNYVHF RNFTEIVRRI NNLEDTSKDK TNE
//
