ID   LPXB_THIDA              Reviewed;         372 AA.
AC   Q3SKM8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Tbd_0798;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96751.1; -; Genomic_DNA.
DR   RefSeq; WP_011311310.1; NC_007404.1.
DR   AlphaFoldDB; Q3SKM8; -.
DR   SMR; Q3SKM8; -.
DR   STRING; 292415.Tbd_0798; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; tbd:Tbd_0798; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_4; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000008291; 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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..372
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255229"
SQ   SEQUENCE   372 AA;  40189 MW;  79246C5A6014C2CA CRC64;
     MVAGEASGDL LGAHFFDALK KNRPGLTAAG IAGPRMVEAG VKAIYPSEKL AVNGYVEVLR
     HLPELLWIRA RITRHFLRER PRVFVGIDAP DFNFTLEAAL KRAGVPTIHF VSPSIWAWRP
     ERIERIKQAV SHMLVVFPFE EAIYRDAGIP VSYVGHPLAD VIPLQAPTGA ARATLGLGDG
     PIVALLPGSR LSEVDRHARL MLEAAMQVRA KEMDVRFVLP AASEAARERI ARAAQGLDLP
     LTVLAGRSHQ ALAACDVAVV ASGTATLEAA LFKKPMVITY RVPALTARLM RKKALLPWIG
     LPNILARDFV VPERVQEAAT PDALAADVLA WLGDAARRAA LAVTFDALHR DLRQGASARI
     AAAIAPYLEA AR
//