LPXB_ALKEH
ID LPXB_ALKEH Reviewed; 382 AA.
AC Q0A7J2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Mlg_1851;
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000453; ABI57195.1; -; Genomic_DNA.
DR RefSeq; WP_011629589.1; NC_008340.1.
DR AlphaFoldDB; Q0A7J2; -.
DR SMR; Q0A7J2; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR PRIDE; Q0A7J2; -.
DR EnsemblBacteria; ABI57195; ABI57195; Mlg_1851.
DR KEGG; aeh:Mlg_1851; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001962; 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..382
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000049383"
SQ SEQUENCE 382 AA; 41866 MW; 6C6A8414633175F4 CRC64;
MRVALVAGEH SGDRLGAGLI RAIRARCPEA EFDGVGGPLM QAEGLRSHYP MEALSVMGLV
EVLRHLPRLL RIRRDLVARY RTDPPDVFVG IDLPDFNLSI ERRLKAVGVP TVHYVSPQVW
AWRQGRVRTI GRSVDRILAL YPFEAEFYRR HGVPVDFVGH PAADRFPLQP DAGAARAALG
LVDDGGGPWV ALLPGSRLGE VQRHAELYAR TVARLRERQP DVRFIAPLAW PGLRAVFYEA
LVQQGVSDAV QLFEGRADEV MAAADVVLTA SGTATLEAML LKRPMVVAYR LAPLTFWLMK
RLVRVSHVSQ PNLLAGEGLV EEYLQDAATP DNLAYALYRL LNDEPRSAYL RARFAELHGT
LRRGADGQAA AAVLAAAGGN GS
