LPXD_ACIBY
ID LPXD_ACIBY Reviewed; 356 AA.
AC B0V6F7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=ABAYE1585;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_00523};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
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DR EMBL; CU459141; CAM86482.1; -; Genomic_DNA.
DR RefSeq; WP_000868103.1; NC_010410.1.
DR AlphaFoldDB; B0V6F7; -.
DR SMR; B0V6F7; -.
DR EnsemblBacteria; CAM86482; CAM86482; ABAYE1585.
DR GeneID; 66396913; -.
DR KEGG; aby:ABAYE1585; -.
DR HOGENOM; CLU_049865_0_1_6; -.
DR OMA; QIQIAHN; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002446; Chromosome.
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 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 PANTHER; PTHR43378; PTHR43378; 1.
DR Pfam; PF00132; Hexapep; 3.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Repeat; Transferase.
FT CHAIN 1..356
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_1000127658"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 356 AA; 38400 MW; A653D4C4FB2A3692 CRC64;
MKVQQYRLDE LAHLVKGELI GEGSLQFSNL ASLENAEVNH LTFVNGEKHL DQAKVSRAGA
YIVTAALKEH LPEKDNFIIV DNPYLAFAIL THVFDKKISS TGIESTAQIH PSAVISETAY
IGHYVVIGEN CVVGDNTVIQ SHTKLDDNVE VGKDCFIDSH VTITGGSKLR DRVRIHSSTV
IGGEGFGFAP YQGKWHRIAQ LGSVLIGNDV RIGSNCSIDR GALDNTILED GVIIDNLVQI
AHNVHIGSNT AIAAKCGIAG STKIGKNCIL AGACGVAGHL SIADNVTLTG MSMVTKNISE
AGTYSSGTGL FENNHWKKTI VRLRQLADVP LTQITKRLDH IQAQIESLES TFNLRK