LPXD_PSEA7
ID LPXD_PSEA7 Reviewed; 353 AA.
AC A6V1E2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=PSPA7_1493;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) 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; CP000744; ABR81687.1; -; Genomic_DNA.
DR RefSeq; WP_003153757.1; NC_009656.1.
DR AlphaFoldDB; A6V1E2; -.
DR SMR; A6V1E2; -.
DR EnsemblBacteria; ABR81687; ABR81687; PSPA7_1493.
DR KEGG; pap:PSPA7_1493; -.
DR HOGENOM; CLU_049865_0_1_6; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001582; 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; 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; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Repeat; Transferase.
FT CHAIN 1..353
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_1000050950"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 353 AA; 36240 MW; E94284619CD4B033 CRC64;
MMSTLSYTLG QLAAHVGAQV RGDADLPIQG LATLQEAGPA HLSFLANPQY RKYLPESRAG
AVLLTAADAD GFAGTALVVA NPYLAYASLS HLFDRKPRAA AGIHPTAIVA ADAEVDPSAS
VGAYAVIESG ARIGAGVSIG AHCVIGARSV IGEGGWLAPR VTLYHDVNIG ARVSIQSGAV
IGGEGFGFAN EKGVWQKIAQ IGGVTIGDDV EIGANTTIDR GALSDTLIGN GVKLDNQIMI
AHNVQIGDHT AMAACVGISG SAKIGRHCML AGGVGLVGHI EICDNVFVTG MTMVTRSITE
PGSYSSGTAM QPAAEWKKSA ARIRQLDDMA RRLQQLEKRL AAVTSSGDAS SDA