ID A0A0U5KXX0_9GAMM Unreviewed; 340 AA.
AC A0A0U5KXX0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000256|HAMAP-Rule:MF_00523};
DE AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000256|HAMAP-Rule:MF_00523,
GN ECO:0000313|EMBL:CUU23049.1};
GN ORFNames=EM595_0813 {ECO:0000313|EMBL:CUU23049.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU23049.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as
CC the acyl donor. Is involved in the biosynthesis of lipid A, a
CC phosphorylated glycolipid that anchors the lipopolysaccharide to the
CC outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-
CC 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
CC Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:71573,
CC ChEBI:CHEBI:78474, ChEBI:CHEBI:78847; Evidence={ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_00523};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000256|HAMAP-
CC Rule:MF_00523}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00523}.
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DR EMBL; LN907827; CUU23049.1; -; Genomic_DNA.
DR RefSeq; WP_067428114.1; NZ_LN907827.1.
DR AlphaFoldDB; A0A0U5KXX0; -.
DR STRING; 1619313.EM595_0813; -.
DR KEGG; ege:EM595_0813; -.
DR PATRIC; fig|1619313.3.peg.848; -.
DR OrthoDB; 9784739at2; -.
DR UniPathway; UPA00359; UER00479.
DR Proteomes; UP000059419; Chromosome 1.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03352; LbH_LpxD; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR HAMAP; MF_00523; LpxD; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR007691; LpxD.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR NCBIfam; TIGR01853; lipid_A_lpxD; 1.
DR PANTHER; PTHR43378; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR43378:SF2; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00132; Hexapep; 3.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00523};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_00523};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00523};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00523}; Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00523}.
FT DOMAIN 22..89
FT /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT acyltransferase non-repeat region"
FT /evidence="ECO:0000259|Pfam:PF04613"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 340 AA; 36130 MW; 0933F438EC7305C9 CRC64;
MPSIRLADLA QQLDAELHGD GDIVISGIAS MQSAKTDHIT FLANSRYREQ LASCQASAVV
LTEADLEWCK SAALIVKDPY LTYARMAQLL DTTPQPASNI APSAVIDPTA TLGENVAIGA
NAVIESDVVL GDNVVIGAGC FVGKKTRIGA HSRLWANVTV YHEIEIGERC LIQSGTVIGA
DGFGYANDRG NWVKIPQLGA VIIGDRVEIG ACTTIDRGAL DDTRIGNGVI IDNQCQIAHN
VMIGDNTAVA GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV
YSSGIPLQPN KTWRKTAALV MNIDEISKRL KTIERKVNKD
//
