LPXD_SYNPW
ID LPXD_SYNPW Reviewed; 358 AA.
AC A5GKW4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=SynWH7803_1153;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT971583; CAK23579.1; -; Genomic_DNA.
DR RefSeq; WP_011933061.1; NC_009481.1.
DR AlphaFoldDB; A5GKW4; -.
DR SMR; A5GKW4; -.
DR STRING; 32051.SynWH7803_1153; -.
DR EnsemblBacteria; CAK23579; CAK23579; SynWH7803_1153.
DR KEGG; syx:SynWH7803_1153; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_0_3; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001566; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
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; 2.
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; Reference proteome; Repeat; Transferase.
FT CHAIN 1..358
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_1000050963"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 358 AA; 36908 MW; 0680BB541F4A9940 CRC64;
MRFSQLIAVL KNGDAGVLST SEGRDPELRG AASLERATAD QLSFLEKGNA LVGSLESSEA
GAVLIPDQQE LRELAERLQL AWAVCGDPRL AFAEALEQLH PKPSPQAGIH ASAVIADRVQ
LGAGVSIGAR VCIGDDTRIG PRTVIHPGVV IYGNVDIGEG CELHANAVLH PGSRIGDRCV
VHSNAVVGSE GFGFVPTAKG WRKMPQTGLV VLEDGVEVGC GSTIDRPSVG ETRIGSGTKI
DNLVQIGHGV VTGRGCALAS QVGIAGGAQL GHGVILAGQV GVANRAVIGD RAIASSKSGI
HGEVAAGEVV SGYPAIPNRL WLRCSAAFSK LPEMAKQLRE LKKQVSSEAT GGSIEADQ
