LPXB_XANOM
ID LPXB_XANOM Reviewed; 432 AA.
AC Q2P4B8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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}; OrderedLocusNames=XOO1854;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE68609.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2P4B8; -.
DR SMR; Q2P4B8; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR KEGG; xom:XOO1854; -.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
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..432
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000255235"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 46688 MW; DD206C883AF08D24 CRC64;
MTGIGNQTSG IETGVHDRAP ADGEPTALPI SHSPLPIPGA HARPPRFALI AGEASGDILG
AGLIAQLRLR YPNAEFVGIG GDAMRGAGCQ TWFDASELAV MGLTEVLRHL PRLLKLRSAF
RERVLAWKPD VFIGIDAPDF NLPVERWLKQ RGIKTVHYVS PSVWAWREKR AEKIAVSADL
VLCLFPMEPP IYAKHGVDAR FVGHPMADDI AYQADRDAAR ATLGLSASST VLAVLPGSRH
GEISRLGDTF LQAAWLVCEH IPNLHVLVPA ANAGCKQLLA EQLSRSSLPV MRSHLINGQA
RTAMLAADVV LLASGTATLE AMLVKRPMVV GYKVAPLTYR IVKLLGLIKV NRYALPNILA
NDDLAPELMQ DDCMPERLCV ALLDWLKHPA KVAALQPRYL ALHAALRRDA SARAAEAVAG
LLQGRDWSGA NI