(data stored in ACNUC14238 zone)

SWISSPROT: LPXB_AQUAE

ID   LPXB_AQUAE              Reviewed;         356 AA.
AC   O67420;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=aq_1427;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-N,3-O-bis(3-hydroxytetradecanoyl)-alpha-D-glucosaminyl
CC         1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-
CC         alpha-D-glucosamine = H(+) + lipid A disaccharide (E. coli) +
CC         UDP; Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC         EC=2.4.1.182;
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.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
DR   EMBL; AE000657; AAC07386.1; -; Genomic_DNA.
DR   PIR; B70424; B70424.
DR   RefSeq; NP_213985.1; NC_000918.1.
DR   RefSeq; WP_010880923.1; NC_000918.1.
DR   SMR; O67420; -.
DR   STRING; 224324.aq_1427; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAC07386; AAC07386; aq_1427.
DR   GeneID; 1192951; -.
DR   KEGG; aae:aq_1427; -.
DR   PATRIC; fig|224324.8.peg.1116; -.
DR   eggNOG; ENOG4105D0V; Bacteria.
DR   eggNOG; COG0763; LUCA.
DR   HOGENOM; HOG000018004; -.
DR   InParanoid; O67420; -.
DR   KO; K00748; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   BioCyc; AAEO224324:G1G15-1019-MONOMER; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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;
DR   PRODOM; O67420.
DR   SWISS-2DPAGE; O67420.
KW   Complete proteome; Glycosyltransferase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN         1    356       Lipid-A-disaccharide synthase.
FT                                /FTId=PRO_0000190151.
SQ   SEQUENCE   356 AA;  41300 MW;  1B4CFBA5F409CD68 CRC64;
     MKKIFLSLAD RSASNYVYEI LKEGFEEYEI YGLTDEKLEK IGVKSVARYS EISTVGLIEA
     LPKVFKFLKI YRKILKNLKN TDTLIACDAP ALNLRLIKDA RKLGVKRIIY FISPQVWAWK
     PKRAEIIANY CDHVIVILPF EKKIYRKFPN LKVHYVGHPL VDLVKPQKTK EEFMKAFKKE
     PLPLLLGSRE GEIRRHVKLL KGIIEELKKS FDVISPTFRE FSKFIERELK VKTLTYEGAS
     YDCFFYSKAS LIASGTASLE AGIAGNPHVV YYKVNPITYF LGKRLVKVPY ISLVNILLKE
     EVVPEFIQKS SDEILKGFEK VYKNEEEIKE KLGTLKFILG ERFVIRKLRE LFLEIV
//

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