LPXB_VIBC3
ID LPXB_VIBC3 Reviewed; 379 AA.
AC A5F627; C3M3K4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=VC0395_A1838, VC395_2363;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000627; ABQ20419.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10353.1; -; Genomic_DNA.
DR RefSeq; WP_001081509.1; NZ_JAACZH010000008.1.
DR AlphaFoldDB; A5F627; -.
DR SMR; A5F627; -.
DR STRING; 345073.VC395_2363; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; ABQ20419; ABQ20419; VC0395_A1838.
DR GeneID; 57740870; -.
DR KEGG; vco:VC0395_A1838; -.
DR KEGG; vcr:VC395_2363; -.
DR PATRIC; fig|345073.21.peg.2278; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000249; Chromosome 2.
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..379
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000072226"
SQ SEQUENCE 379 AA; 42250 MW; 646808F3DDFA3CCE CRC64;
MNRPLRIGIV VGELSGDTLG EGFIKAIRAR YPDAEFVGIG GPKMNALGCQ SLFDMEELAV
MGLVEVLGRL PRLLKVKAEL VKYFTANPPD VFVGIDAPDF NLRLELSLKQ AGIKTVHYVS
PSVWAWRQNR IHGIAAATHL VLAFLPFEKA FYDKFNVPCE FIGHTLADSI PLASDKLAAR
QLLGLDEQRR WLAVLPGSRG SEMKMLAEPF IATCQKLQAR YPDLGFVVAL VNAKRRAQFE
QAWQQVAPEL NFVLVDDTAR NVITAADAVM LASGTVALEC MLLKRPMVVG YRVNAFTAFL
AKRLLKTPYV SLPNILAGEE LVKELLQDHC TVDNLYHEVS RLLESDNQAL MDKFTEMHQW
IRKDADQQAA QAVLHLIQK
