LPXD_YEREN
ID LPXD_YEREN Reviewed; 340 AA.
AC P32203;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
DE AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; Synonyms=firA;
OS Yersinia enterocolitica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EH902;
RX PubMed=8293817; DOI=10.1016/0014-5793(94)80211-4;
RA Vuorio R., Haerkonen T., Tolvanen M., Vaara M.;
RT "The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of
RT lipid A biosynthesis is conserved in various bacteria.";
RL FEBS Lett. 337:289-292(1994).
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: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 -!- 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:0000255|HAMAP-
CC 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:0000255|HAMAP-
CC 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; Z25463; CAA80951.1; -; Genomic_DNA.
DR PIR; S41752; S41752.
DR AlphaFoldDB; P32203; -.
DR SMR; P32203; -.
DR STRING; 1443113.LC20_01205; -.
DR eggNOG; COG1044; Bacteria.
DR BRENDA; 2.3.1.191; 6741.
DR UniPathway; UPA00359; UER00479.
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 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 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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 3.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..340
FT /note="UDP-3-O-(3-hydroxymyristoyl)glucosamine N-
FT acyltransferase"
FT /id="PRO_0000059716"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 340 AA; 35709 MW; DA5C6CF630E1675A CRC64;
MPSIRLADLA QQLDAQVHGD GDLVITGIAS MHSAEPSQIT FLSNSRYQEQ LATCNAGAVV
LTEADLPFCK SAALVVKNPY LTYARMAQIM DTTPQPAQNI APGAVISPQA TLGENVSIGA
NAVIESGVVL GDNVVIGAGC FIGKNTHIGA GSRLWANVSV YHEVVIGQNC LIQSGTVIGA
DGFGYANDRG NWIKIPQLGS VHIGDRVEIG ACTTIDRGAL DNTIIGNGVI IDNQCQIAHN
VVIGDNTAVA GGVIMAGSLK VGRYCMIGGA SVINGHMEIC DKVTITGMGM VMRPITEPGL
YPSGIPLQPN KVWRKTAALV MNIDGINKRL KAIERKIDKE
