ID   LPXB_ARATH              Reviewed;         460 AA.
AC   F4IF99; Q500V1; Q9SJB5;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Probable lipid-A-disaccharide synthase, mitochondrial;
DE            EC=2.4.1.182;
DE   AltName: Full=Protein LIPID X B;
DE            Short=AtLpxB;
DE   Flags: Precursor;
GN   Name=LPXB; OrderedLocusNames=At2g04560; ORFNames=T1O3.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis cDNA clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PATHWAY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=21709257; DOI=10.1073/pnas.1108840108;
RA   Li C., Guan Z., Liu D., Raetz C.R.;
RT   "Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that
RT   of Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:11387-11392(2011).
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 in bacteria anchors the
CC       lipopolysaccharide to the outer membrane of the cell. Lipid A-like
CC       molecules in plants may serve as structural components of the outer
CC       membranes of mitochondria and/or chloroplasts, or may be involved in
CC       signal transduction or plant defense responses (Potential).
CC       {ECO:0000305}.
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;
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:0000269|PubMed:21709257}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21709257}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but plants lacking LPXB accumulate high levels of 2,3-
CC       diacylglucosamine-1-phosphate and UDP-2,3-diacylglucosamine.
CC       {ECO:0000269|PubMed:21709257}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD25824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAY34177.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC006951; AAD25824.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC05847.1; -; Genomic_DNA.
DR   EMBL; BT022116; AAY34177.1; ALT_FRAME; mRNA.
DR   PIR; H84458; H84458.
DR   RefSeq; NP_178535.3; NM_126487.4.
DR   AlphaFoldDB; F4IF99; -.
DR   SMR; F4IF99; -.
DR   STRING; 3702.AT2G04560.1; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   iPTMnet; F4IF99; -.
DR   PaxDb; F4IF99; -.
DR   PRIDE; F4IF99; -.
DR   ProteomicsDB; 238590; -.
DR   EnsemblPlants; AT2G04560.1; AT2G04560.1; AT2G04560.
DR   GeneID; 814998; -.
DR   Gramene; AT2G04560.1; AT2G04560.1; AT2G04560.
DR   KEGG; ath:AT2G04560; -.
DR   Araport; AT2G04560; -.
DR   TAIR; locus:2058329; AT2G04560.
DR   eggNOG; ENOG502QTT8; Eukaryota.
DR   HOGENOM; CLU_036577_2_0_1; -.
DR   InParanoid; F4IF99; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1041189at2759; -.
DR   BRENDA; 2.4.1.182; 399.
DR   UniPathway; UPA00359; UER00481.
DR   PRO; PR:F4IF99; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IF99; baseline and differential.
DR   Genevisible; F4IF99; AT.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IMP:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR   GO; GO:2001289; P:lipid X metabolic process; IMP:UniProtKB.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF02684; LpxB; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..460
FT                   /note="Probable lipid-A-disaccharide synthase,
FT                   mitochondrial"
FT                   /id="PRO_0000421460"
SQ   SEQUENCE   460 AA;  51465 MW;  87109A715C617EDA CRC64;
     MMFQITKSKL RFPLSTFTKR YSSFQAAKSV IDKAAIDGEL RVFIVSGEVS GDNIGSRLMS
     SLKKLSPLPI RFNGVGGSLM CKKGLNSLFP MEDLAVMGVW ELLPHLYKFR VKLKETIDAA
     VKFKPHVVVT VDSKGFSFRL LKELRARYKQ QRLENCSVHF HYVAPSFWAW KGGESRLGGL
     SEFVDHLFCI LPNEERVCRE HGVEATFVGH PVLEDASEFD LVRRCKPQEL KLEGLSFSEH
     SIPSDSTVIS VLPGSRLQEV ERMLPIFSKA MKLLKDPFPK LVTLIHVASN NQVDHYIGES
     FSEWPVPAIL VPSGSTQLKY DAFGASQAAL CTSGTVAVEL QLAHLPSLVA YRAHFLTELL
     IRYKAKIPYI SLPNILLDSP IIPEALFQAC NPSNLASILE RLLLDEKMRE RQVVGAEKLI
     QLLHPSESRM GNSIHCTGLE SHRYTPSILA ASTILSYARR