LPXB_SHESW
ID LPXB_SHESW Reviewed; 384 AA.
AC A1RLL4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=Sputw3181_2742;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000503; ABM25559.1; -; Genomic_DNA.
DR RefSeq; WP_011790015.1; NC_008750.1.
DR AlphaFoldDB; A1RLL4; -.
DR SMR; A1RLL4; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR GeneID; 45041793; -.
DR KEGG; shw:Sputw3181_2742; -.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002597; 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..384
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000049421"
SQ SEQUENCE 384 AA; 42409 MW; B746AF9CC8C68D25 CRC64;
MSKKSQLVFA MVAGELSGDI LGAGLMAALQ KSHPDARFVG IGGPRMEALG FESLFAMEEL
AVMGIVEVLS RLPRLLKVRA SLIKDITALK PDCFIGIDAP DFNIGLELKL KARGIKTVHY
VSPSVWAWRP KRIFKIAKAT HMVLSLLPFE KAFYDKHQVP CTFVGHTLAD DIPLRSDKAA
ARQLLELDAD AEYLAILPGS RGGELKQLAE PFVKAALLIK ENFPDIRFVT PLVNQKRRDQ
FEQALKDHAP DLEIHMVEGK SREVMTAADG ILLASGTATL EAMLVKRPMV VAYRVSPLTY
RIAKSMMQVN RFSLPNLLAG KDVVPELIQD DCTPEKIAAA VTVELNRDFA PLNAEFERLH
QMLRCDASQK AADAVMRLVE TKEG