LPXB_TRIL1
ID LPXB_TRIL1 Reviewed; 383 AA.
AC B3E4H8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=Glov_0767;
OS Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS lovleyi).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Trichlorobacter.
OX NCBI_TaxID=398767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA Ritalahti K.M., Loeffler F.E., Richardson P.;
RT "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL Submitted (MAY-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=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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001089; ACD94493.1; -; Genomic_DNA.
DR RefSeq; WP_012468849.1; NC_010814.1.
DR AlphaFoldDB; B3E4H8; -.
DR SMR; B3E4H8; -.
DR STRING; 398767.Glov_0767; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; ACD94493; ACD94493; Glov_0767.
DR KEGG; glo:Glov_0767; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_1_7; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002420; 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..383
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000123050"
SQ SEQUENCE 383 AA; 41770 MW; 482BF35BC063C6D1 CRC64;
MAVGRPKRVM IVAGEASGDI YGAGLVRAVQ AADPAFSFFG IGGPRMREAG CETLVDSADM
AVVGLVEVLK HFDVIAAAFL KLKKILLEDP PDLLILIDYP GFNLRLGKVA KKAGVKVLYY
ISPQIWAWRQ GRVKKIKRLV DHMAVILPFE VPFYEQAGVP VSFVGHPMAD LVEVSLTRDQ
AATSFGLDTS RQIVGLFPGS RRSEVSRLLP TILEAARLLQ QCLPGLQFVL PLASTLSDDD
LAPWLEGCEL PITVTRDRIH DLMRACDAVI SVSGTVTLEI ALVGTPLVII YKLSPLTFQL
AKRLVKVEHI GLCNIVAGET VARELIQEEA SPEQIAGEIG RLLRDAEYNT AFRERLTHVR
ERLGGGGADR RMAGLVLSMV EQS
