LPXD_ACIBS
ID LPXD_ACIBS Reviewed; 356 AA.
AC B0VMV2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=ABSDF1688;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
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; CU468230; CAP01028.1; -; Genomic_DNA.
DR PDB; 4E75; X-ray; 2.85 A; A/B/C/D/E/F=2-355.
DR PDB; 4E79; X-ray; 2.66 A; A/B/C=2-355.
DR PDBsum; 4E75; -.
DR PDBsum; 4E79; -.
DR AlphaFoldDB; B0VMV2; -.
DR SMR; B0VMV2; -.
DR EnsemblBacteria; CAP01028; CAP01028; ABSDF1688.
DR KEGG; abm:ABSDF1688; -.
DR HOGENOM; CLU_049865_0_1_6; -.
DR OMA; QIQIAHN; -.
DR BRENDA; 2.3.1.191; 98.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001741; 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 1: Evidence at protein level;
KW 3D-structure; 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_1000127656"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:4E79"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4E79"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4E79"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:4E79"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4E79"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4E79"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:4E79"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:4E79"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:4E79"
SQ SEQUENCE 356 AA; 38484 MW; BF15F948205840F6 CRC64;
MKVQQYRLDE LAHLVKGELI GEGSLQFSNL ASLENAEVNH LTFVNGEKHL DQAKVSRAGA
YIVTAALKEH LPEKDNFIIV DNPYLAFAIL THVFDKKISS TGIESTARIH PSAVISETAY
IGHYVVIGEN CVVGDNTVIQ SHTKLDDNVE VGKDCFIDSY VTITGSSKLR DRVRIHSSTV
IGGEGFGFAP YQGKWHRIAQ LGSVLIGNDV RIGSNCSIDR GALDNTILED GVIIDNLVQI
AHNVHIGSNT AIAAKCGIAG STKIGKNCIL AGACGVAGHL SIADNVTLTG MSMVTKNISE
AGTYSSGTGL FENNHWKKTI VRLRQLADVP LTQITKRLDH IQAQIESLES TFNLRK
