ID A0A3N4UN49_9RHOB Unreviewed; 362 AA.
AC A0A3N4UN49;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=EDD53_0567 {ECO:0000313|EMBL:RPE71448.1};
OS Pacificibacter maritimus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pacificibacter.
OX NCBI_TaxID=762213 {ECO:0000313|EMBL:RPE71448.1, ECO:0000313|Proteomes:UP000269689};
RN [1] {ECO:0000313|EMBL:RPE71448.1, ECO:0000313|Proteomes:UP000269689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 104731 {ECO:0000313|EMBL:RPE71448.1,
RC ECO:0000313|Proteomes:UP000269689};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-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}.
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:RPE71448.1}.
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DR EMBL; RKQK01000001; RPE71448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4UN49; -.
DR OrthoDB; 9784739at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000269689; 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; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR007691; LpxD.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
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; PF14602; Hexapep_2; 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};
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:UP000269689};
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 ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 362 AA; 36581 MW; C6B228D707DD02AA CRC64;
MTRIKLSDLA QRLNAPFVGD GSISVSGASE PATAKRDDLA LAMDPKFAAD LTKGAARVAV
LWQGADWQSL GLEGAILVSR GRLAMAGITA GFDAGLSLPA GVHPSAVIDE TATIATDVKI
GPLVVVGAGA VIGAGSQIAP HVSIGAGVQI GDDAVIHAGV RIGAQAKIGA RIHIQAGAVI
GSDGFSFVTQ DKSAVEETRE SLGADVQAKG QSWLRIASIG GVVIGDDVEI GANVTIDQGT
IRPTQIGSGS KLDNQVHIGH NVIVGAHCLL CGQVGIAGST VLGDFCVMGG QAGAADNITI
GQGAIIGAGS GVLSNVAKGK AMMGYPAVAM QTHVDMYKSL RRLPRILKTL AKEASQSHKD
KT
//
