ID   LPXB_MAGSA              Reviewed;         390 AA.
AC   Q2W4D7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=amb2484;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE51288.1; -; Genomic_DNA.
DR   RefSeq; WP_011384865.1; NC_007626.1.
DR   AlphaFoldDB; Q2W4D7; -.
DR   SMR; Q2W4D7; -.
DR   STRING; 342108.amb2484; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; BAE51288; BAE51288; amb2484.
DR   KEGG; mag:amb2484; -.
DR   HOGENOM; CLU_036577_3_0_5; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000007058; 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..390
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255196"
SQ   SEQUENCE   390 AA;  41913 MW;  6654FB66F2025349 CRC64;
     MLIYLIAGEP SGDLLGGRLM AALKERLGEG VSFAGIGGES MRAEGLTSLF PMTELSVMGL
     VEVLPRIPKI LRRVKQTISD IETKRPDALV TIDSWGFNGR IQAGLKARGV PVPRIHYVAP
     MVWAWKSGRT KTLARVLDLL LTLLPNEPEW FEKEGLKTLH VGHPVIEGAA SRGDGAAFRV
     RHGFAPDRKL LCVLPGSRHS ETAKLLAPFG ETIALLARRF PDLAVVVPTV ETVADEVSQA
     VKSWALPSMV VRGPEKYDAF AACDAALAAS GTVALELAMA RLPAVITYKV SPVSAFIATR
     FLGLSLKFVT LVNILVDEAV MPELLQDDCR PDKLAAAVEH LLTDEAARAL QAAGARRALE
     KLGLGGESPG KRAADAVIDF IRQGKEQRNG