ID   LPXB_AZOSB              Reviewed;         391 AA.
AC   A1K6Q8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=azo1896;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(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; AM406670; CAL94513.1; -; Genomic_DNA.
DR   RefSeq; WP_011765629.1; NC_008702.1.
DR   AlphaFoldDB; A1K6Q8; -.
DR   SMR; A1K6Q8; -.
DR   STRING; 62928.azo1896; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PRIDE; A1K6Q8; -.
DR   EnsemblBacteria; CAL94513; CAL94513; azo1896.
DR   KEGG; aoa:dqs_2051; -.
DR   KEGG; azo:azo1896; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002588; 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..391
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049384"
SQ   SEQUENCE   391 AA;  43154 MW;  F2B166A1679766F8 CRC64;
     MAPRIAMVAG EASGDLLASH LIRAIRARVP DAEFFGIGGP KMQAEGFDAR WPCELLAVHG
     YVDALKRYRE LSGIRKKLLK QVRRERPDAF IGVDAPDFNL WLEGKIKAAG IPAIHFVSPS
     IWAWRGGRIK RIARSVTRML CMFPFEPELY ERAGVPVSYV GHPLADVFPL EPDRAAARER
     LDIAPERKVV ALLPGSRQSE VRNLGELFIE TAAMLAQRHP DVLFLVPLAT RETRELFSAA
     LARNKGDELP LRMLFGHAVD AMTAADAVLV ASGTASLEAA LLKRPMVITY RMGKWQYRLM
     KRMAYLPWIG LPNILCREGL VPELVQDDAT PPKLADALER WLVDPAACAA LTERFTALHH
     SLRQNTAEKA AAAVLPYLSS SASCQPVSVS A