LPXD_XANOM
ID LPXD_XANOM Reviewed; 337 AA.
AC Q2P4B5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=XOO1857;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE68612.1; -; Genomic_DNA.
DR RefSeq; WP_011408323.1; NC_007705.1.
DR AlphaFoldDB; Q2P4B5; -.
DR SMR; Q2P4B5; -.
DR KEGG; xom:XOO1857; -.
DR HOGENOM; CLU_049865_0_1_6; -.
DR OMA; QIQIAHN; -.
DR UniPathway; UPA00973; -.
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..337
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000264460"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 337 AA; 34843 MW; 059CAA38E2F4973B CRC64;
MRLTASAIAG QFGLTVLGDG STEVSGVATL AHAGAGQLSF LSNPRYRPQL ADSQAAVVVL
RADDAEAAKG TALVAKDPYT AFAKIAALFD VAQVCEPGIH PSAFIDPTAQ VSPGAHVGPF
VSIGARSRVG DGCVIGTGSL IGADCVVDDG SELLARVTLV TRVRLGKRVR IHPGAVIGAD
GFGLAMDAGH WIKVPQLGGV VIGDDCEIGA NTCIDRGALE DTVLEEDVRV DNLVQIAHNC
RIGAHSAIAG CSGIAGSAKI GRYCLLGGHV GVVGHLEICD KVVITGKSVV RNSINEPGEY
SSGTPLTDNR TWRKNAARFK QLDVLARRIL AVGKEKE