(data stored in ACNUC7421 zone)

SWISSPROT: LPXB_ECODH

ID   LPXB_ECODH              Reviewed;         382 AA.
AC   B1XD51;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 59.
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};
GN   OrderedLocusNames=ECDH10B_0162;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC       diacylglucosamine-1-phosphate to form lipid A disaccharide, a
CC       precursor 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: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-
CC       alpha-D-glucosamine + 2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-
CC       alpha-D-glucosaminyl 1-phosphate = UDP + 2-N,3-O-bis((3R)-3-
CC       hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis((3R)-
CC       3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-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}.
DR   EMBL; CP000948; ACB01360.1; -; Genomic_DNA.
DR   RefSeq; WP_000139654.1; NC_010473.1.
DR   ProteinModelPortal; B1XD51; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ACB01360; ACB01360; ECDH10B_0162.
DR   KEGG; ecd:ECDH10B_0162; -.
DR   eggNOG; ENOG4105D0V; Bacteria.
DR   eggNOG; COG0763; LUCA.
DR   HOGENOM; HOG000018003; -.
DR   KO; K00748; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00359; UER00481.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
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;
DR   PRODOM; B1XD51.
DR   SWISS-2DPAGE; B1XD51.
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN         1    382       Lipid-A-disaccharide synthase.
FT                                /FTId=PRO_1000191475.
SQ   SEQUENCE   382 AA;  42382 MW;  12C76B6ECA438B47 CRC64;
     MTEQRPLTIA LVAGETSGDI LGAGLIRALK EHVPNARFVG VAGPRMQAEG CEAWYEMEEL
     AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY
     VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNA
     ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ
     FERIKAEVAP DLSVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
     WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE
     LHQQIRCNAD EQAAQAVLEL AQ
//

If you have problems or comments...

PBIL Back to PBIL home page