LPXB_SYNC1
ID LPXB_SYNC1 Reviewed; 392 AA.
AC Q3A550;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Pcar_1258;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
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; CP000142; ABA88507.1; -; Genomic_DNA.
DR RefSeq; WP_011340982.1; NC_007498.2.
DR AlphaFoldDB; Q3A550; -.
DR SMR; Q3A550; -.
DR STRING; 338963.Pcar_1258; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; ABA88507; ABA88507; Pcar_1258.
DR KEGG; pca:Pcar_1258; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_1_7; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002534; 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..392
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000255204"
SQ SEQUENCE 392 AA; 42903 MW; 95CE64BCA319AD64 CRC64;
MHEVKQPRRI MVVTGEASGD LHGAHLIEAA GKVDPGLSFF GVGGACMAKA GCEILIPGED
LAVMGLVEVL GHFPTIWRAF RKLKKILHGP QRPDALVLID FAEFNLLLAA QAKKAGVPVL
YYVSPQVWAW RRGRVRRIAS VVDRLAAIFP FEPELYQGLD IDVEYVGHPL LDEFAITCER
DAFLRRLGLD PARQVIGLFP GSRKNELKYI AETILQSAVK LREKHPDAQF LLPVASSFRR
QDIEALVAPY GLPVTVVDEP IYDVINACDA VISVSGTVTL QVALVGTPMA IVYKMAPLSF
AIGKRLIRVP HIGLANIVAG RGVVKEFIQE DATPAMISRE IDAILTDAEY NRSIRGGLAT
VQQRMGEGGC AARVARMVSE LCREIPGKER MV