LPXB_BRADU
ID LPXB_BRADU Reviewed; 392 AA.
AC Q89KQ7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, 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}; OrderedLocusNames=bll4847;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC50112.1; -; Genomic_DNA.
DR RefSeq; NP_771487.1; NC_004463.1.
DR RefSeq; WP_011087615.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89KQ7; -.
DR SMR; Q89KQ7; -.
DR STRING; 224911.27353111; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; BAC50112; BAC50112; BAC50112.
DR GeneID; 64024600; -.
DR KEGG; bja:bll4847; -.
DR PATRIC; fig|224911.5.peg.4927; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_5; -.
DR InParanoid; Q89KQ7; -.
DR OMA; PTVWAWR; -.
DR PhylomeDB; Q89KQ7; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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_0000190155"
SQ SEQUENCE 392 AA; 43262 MW; 7956C1EBD78B9C73 CRC64;
MMQGRDPKRK IFLIATEESG DRLGSALMKV LRQRLGDGVQ FEGVGGRTMA REGLETLFPI
EELSIVGFAA VVQQLPKILR LIRETADAVL EAVPDALVII DSPDFTHRVA RRVRARNPAI
PIVDYVSPQL WAWRPGRART MLGYVDHVLG LLPFEPEEYR KLGGPPCSYV GHPLIEQLGS
LRPNAEEQKR RNSELPVLLV LPGSRRSEIR HHIEVFGAAL GRLQAEGRAF ELMLPTMPHL
EATVREGIAS WPVKPQIVIG EAEKRAAFRI AHAALAKSGT VTLELALSGI PMVTAYRVGA
IEAFILRRAI RVSSVILANL VIGEDVIPEF LQEDCTPEKL APALSEVLTD SDMRRRQVEA
FARLDTIMST GNKAPSVLAA DIVLATMRKG RR
