LPXB_GEOMG
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 25-MAY-2022, entry version 83.
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=Gmet_2350;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
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 EnsemblBacteria; ABB32575; ABB32575; Gmet_2350.
DR KEGG; gme:Gmet_2350; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_1_7; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
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 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; 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