(data stored in ACNUC7421 zone)

SWISSPROT: LPXB_HISS2

ID   LPXB_HISS2              Reviewed;         389 AA.
AC   B0UW62;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 58.
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=HSM_0257;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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(3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-
CC         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         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}.
DR   EMBL; CP000947; ACA31884.1; -; Genomic_DNA.
DR   RefSeq; WP_012341127.1; NC_010519.1.
DR   SMR; B0UW62; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ACA31884; ACA31884; HSM_0257.
DR   GeneID; 31486537; -.
DR   KEGG; hsm:HSM_0257; -.
DR   HOGENOM; HOG000018003; -.
DR   KO; K00748; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   BioCyc; HSOM228400:G1GB8-267-MONOMER; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000008543; 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;
DR   PRODOM; B0UW62.
DR   SWISS-2DPAGE; B0UW62.
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..389
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000080280"
SQ   SEQUENCE   389 AA;  44097 MW;  BB1965D781641EBE CRC64;
     MIDKKNITIG IVAGEVSGDI LGAGLIRALK IQYPQARFIG IAGKNMLAEG CKTLVDMEDI
     AVMGLVEVIK YLPRLLKIRR LVIDTMLAEK PDIFIGIDAP DFNLDIELKL KKQGIKTLHY
     VSPSVWAWRQ KRIFKIAQAT NLVLAFLPFE KAFYDRFNVP CRFVGHTMAD IIDLQPDRQD
     ACFQLNLEPK HRYVAILVGS REAEVQFLTP PFLQTAQLIK QRFPDVQFLV PLVNEKRRKQ
     FEQIKAQIAP HLEVIFLDGQ ARQAMIVAEA SLLASGTASL ECMLCKSPMV VGYKMKPFTY
     FLAKRLVKTK YISLPNLLAD DMLVPEMIQE DCTAEKLAEK LSVYLEQTES GIKNRQHLIQ
     QFTQLHQLIR CDADKQAAQA VIDLLNDEV
//

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