LPXB_ALTMD
ID LPXB_ALTMD Reviewed; 382 AA.
AC B4RVJ5; F2G288;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392};
GN OrderedLocusNames=MADE_1005380;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
CC -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor
CC of lipid A, a phosphorylated glycolipid that anchors the
CC lipopolysaccharide to the outer membrane of the cell.
CC {ECO:0000255|HAMAP-Rule:MF_00392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC glucosamine = a lipid A disaccharide + H(+) + UDP;
CC Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343;
CC EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00392}.
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
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DR EMBL; CP001103; AEA97222.1; -; Genomic_DNA.
DR RefSeq; WP_012517576.1; NC_011138.3.
DR AlphaFoldDB; B4RVJ5; -.
DR SMR; B4RVJ5; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; AEA97222; AEA97222; MADE_1005380.
DR KEGG; amc:MADE_1005380; -.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001870; Chromosome.
DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00392; LpxB; 1.
DR InterPro; IPR003835; Glyco_trans_19.
DR PANTHER; PTHR30372; PTHR30372; 1.
DR Pfam; PF02684; LpxB; 1.
DR TIGRFAMs; TIGR00215; lpxB; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Transferase.
FT CHAIN 1..382
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000191459"
SQ SEQUENCE 382 AA; 42334 MW; 71832D847E3CC0F3 CRC64;
MSKPIRIGMV AGEPSGDILA AGMVAELKRQ YPDAIIEGIG GPNMIDAGFH SLFDMETLSV
MGLVEVLAHL PAILKVKKQL LAHFEQNPPD IFVGVDAPDF NLRVEKALKA RGIKTMHYVS
PTVWAWREKR IHKIAKAANR VLGLFPFEQQ VYDKYHVPYT FVGHTMADAI AIEPDQNAAR
QELGVESNAY VLAVLPGSRR GEVETLLPVF LETIEAIHVK RSDIQFLIPA ANEHRLAQIK
AFLQEANNAE ERLPIQVTQG TSRDAMIASD VILLASGTAT LEAMLCKRPM VAAYLLSPLT
YKIMQRLYKA PFFTLPNLLA NEAIIPELLQ EEVNAENMSN QLLNFFESDN SALIARFTDL
HHTLKCNADK TAAKAVVEEL FA