LPXD_RHILO
ID LPXD_RHILO Reviewed; 351 AA.
AC Q98MC4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=mll0635;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB48189.1; -; Genomic_DNA.
DR RefSeq; WP_010909544.1; NC_002678.2.
DR AlphaFoldDB; Q98MC4; -.
DR SMR; Q98MC4; -.
DR STRING; 266835.14021577; -.
DR EnsemblBacteria; BAB48189; BAB48189; BAB48189.
DR GeneID; 66683990; -.
DR KEGG; mlo:mll0635; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_2_5; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000552; 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; 2.
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..351
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000059694"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 351 AA; 35585 MW; 7D865F67C7C0570F CRC64;
MTDPVFFAPS RRYTAAEVAN LTGSVLVDSG QSDVSIEALA PASEGGANAL VFVDGRRNSA
LMPSLRAAAV LCPAEFANKA PSSVAVLIHP RPQQAFALVG RLLFPTAATP GPMTSETGVS
AHAHIDPTAH VEAGAIIEAG VVIGPGVSIG SGTVIAPNAV IGQSCQIGRD GYVGPGASIQ
YALIGNRVII HGGARIGQDG FGFVGGAKGP ERVPQIGRVV IQDDVEIGSN STVDRGAMSD
TIIGQGTKID NLVQIAHNVR IGRNCIVAGL SGISGSVVVG DNVTMGGGVG LADHLTIGSG
AKLAARSGFM SNVPAGEIWG GYPAQPMAEA MREIAMLRTM ARARKQGKDN G