LPXD_DESVM
ID LPXD_DESVM Reviewed; 343 AA.
AC B8DSI1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=DvMF_2999;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) 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: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; CP001197; ACL09936.1; -; Genomic_DNA.
DR RefSeq; WP_015946617.1; NC_011769.1.
DR AlphaFoldDB; B8DSI1; -.
DR SMR; B8DSI1; -.
DR STRING; 883.DvMF_2999; -.
DR EnsemblBacteria; ACL09936; ACL09936; DvMF_2999.
DR KEGG; dvm:DvMF_2999; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_0_7; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
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..343
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_1000127678"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 343 AA; 35511 MW; 5D4CC033B9E4DD5B CRC64;
MARLLSELAG LLGLELRGED RAIEGVNTLE AAGPAEVSFL ANPKYTHLLA NTRAGAVIVT
AEHADAVPCA LVSTNPYFDF GRTLALFSKP QGSLSGVSDM AFVHPEAELG EGCTVYPFAF
IGPRARIGAG SVLFPGVYVG EDCRVGAGCL LYPNAVLMAG TEIGNGCILH AGVVLGADGF
GFARTDFGIQ KIPQVGTVRL GNDVEVGANT AIDRSVLGVT TVGDSTKIDN LVQIGHNVEM
GRNCLIVSQV GISGSTKVGD DVTMAGQVGV AGHLSIGNGV TLGPKSGVAK SIPDGETMGG
APAVDKATYM RTLTVMPKLP DMYKRIGKLE KELEELKKLA AKE
