ID   LPXB_GEOMG              Reviewed;         384 AA.
AC   Q39T49;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 90.
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=Gmet_2350;
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) 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; CP000148; ABB32575.1; -; Genomic_DNA.
DR   RefSeq; WP_011366042.1; NC_007517.1.
DR   AlphaFoldDB; Q39T49; -.
DR   SMR; Q39T49; -.
DR   STRING; 269799.Gmet_2350; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; gme:Gmet_2350; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_7; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000007073; 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   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..384
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255183"
SQ   SEQUENCE   384 AA;  41622 MW;  B3E98A1B1011F88C CRC64;
     MGTAPNKRVM IVAGEASGDL HGSNLVKEAL RLDPTLSFFG IGGPHMRAAG VETVVDSSEM
     AVVGLVEVLA HFGVIYKAYA TLKRLITTNP PDLLILIDYP DFNMLVAKVA KRAGVKVLYY
     ISPQVWAWRT GRVKKIARLV DRMAVVFPFE VPFYEKAGVP VSFVGHPLAD RVSPSMSRSE
     ALAAFGLDPS RRVVGLFPGS RRGEIARLFP VILESAKLLR DRYPGIQFIL PLASSLTDAD
     IAPHLAASGL EVVVARDKVY DVMQVCDAIA TVSGTVTLEI ALMGVPMVII YTVSPLTYEV
     GKRLIRVDHI GICNIVAGER VVPELIQDEA TAERIAAEIG RYLDDPVHTE KTRAGLARVR
     EKLGSGGCSE RVAGIVLEML GKKR
//