LPXB_BLOPB
ID LPXB_BLOPB Reviewed; 387 AA.
AC Q493B9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=BPEN_292;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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=2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl
CC 1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP;
CC Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC Evidence={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: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 5/6. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
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DR EMBL; CP000016; AAZ40923.1; -; Genomic_DNA.
DR AlphaFoldDB; Q493B9; -.
DR SMR; Q493B9; -.
DR STRING; 291272.BPEN_292; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR PRIDE; Q493B9; -.
DR EnsemblBacteria; AAZ40923; AAZ40923; BPEN_292.
DR KEGG; bpn:BPEN_292; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR BioCyc; CBLO291272:BPEN_RS01435-MON; -.
DR UniPathway; UPA00359; UER00481.
DR Proteomes; UP000007794; 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; Transferase.
FT CHAIN 1..387
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000255161"
SQ SEQUENCE 387 AA; 44034 MW; B97761F9A2CFC254 CRC64;
MSSIVPSMHN NRTIIIGIVA GEASGDILGA GLIRTLKKYL KKVRFFGIGG PCMQSEDMKS
WYNIEELSVM GFAEIVMKLP RLLYIRRNLA RRFINLKPDV FIGIDSPDFN ISLENRLKKR
GIRTIHYVSP SVWAWRKKRI FALKKATDNI LVILPFEKKI YDHFNIPCQF IGHSLADQIP
LNPNKVSARQ KLGIPHDVYC LAVLPGSRIR EIKMLAHDFL VCAKLLKNNF PNLEILVPLT
NQTSIKKFIS VASTSVKYRV LSNQSAWEIM MAADASLVTA GTATLECMLV KCPMVVAYRM
HPLTFMLAKH FINIPWISLP NLLAGHELVK EFIQNNCRPE NLAQTLINLL NNNNQHIVLK
KKFRQLHHSI RCNADEQAAY AVLRLIK
