LPXK_ARATH
ID LPXK_ARATH Reviewed; 395 AA.
AC Q8LEA0; Q9LJV0;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable tetraacyldisaccharide 4'-kinase, mitochondrial;
DE EC=2.7.1.130;
DE AltName: Full=Protein LIPID X 4'-kinase;
DE Short=AtLpxK;
DE Flags: Precursor;
GN Name=LPXK; OrderedLocusNames=At3g20480; ORFNames=K10D20.1;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that in bacteria anchors the lipopolysaccharide to the outer
CC membrane of the cell. Transfers the gamma-phosphate of ATP to the 4'-
CC position of a tetraacyldisaccharide 1-phosphate intermediate (termed
CC DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
CC Lipid A-like molecules in plants may serve as structural components of
CC the outer membranes of mitochondria and/or chloroplasts, or may be
CC involved in signal transduction or plant defense responses (Potential).
CC {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-
CC glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-
CC D-glucosaminyl phosphate} = ADP + {2-N,3-O-bis[(3R)-3-
CC hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl}-(1->6)-{2-N,3-
CC O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate}.;
CC EC=2.7.1.130;
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 6/6. {ECO:0000269|PubMed:21709257}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21709257}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LEA0-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants lacking LPXK accumulate high levels of
CC disaccharide-1-phosphate (DS-1-P). {ECO:0000269|PubMed:21709257}.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01156.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000410; BAB01156.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76385.1; -; Genomic_DNA.
DR EMBL; AY085541; AAM62765.1; -; mRNA.
DR RefSeq; NP_001327104.1; NM_001338484.1.
DR RefSeq; NP_566663.1; NM_112940.3. [Q8LEA0-1]
DR AlphaFoldDB; Q8LEA0; -.
DR SMR; Q8LEA0; -.
DR STRING; 3702.AT3G20480.1; -.
DR PaxDb; Q8LEA0; -.
DR EnsemblPlants; AT3G20480.1; AT3G20480.1; AT3G20480. [Q8LEA0-1]
DR GeneID; 821594; -.
DR Gramene; AT3G20480.1; AT3G20480.1; AT3G20480. [Q8LEA0-1]
DR KEGG; ath:AT3G20480; -.
DR Araport; AT3G20480; -.
DR TAIR; locus:2085765; AT3G20480.
DR eggNOG; ENOG502QRUA; Eukaryota.
DR HOGENOM; CLU_038816_4_0_1; -.
DR OMA; MDDGFQN; -.
DR PhylomeDB; Q8LEA0; -.
DR UniPathway; UPA00359; UER00482.
DR PRO; PR:Q8LEA0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LEA0; baseline and differential.
DR Genevisible; Q8LEA0; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IMP:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001289; P:lipid X metabolic process; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_00409; LpxK; 1.
DR InterPro; IPR003758; LpxK.
DR PANTHER; PTHR42724; PTHR42724; 1.
DR Pfam; PF02606; LpxK; 1.
DR TIGRFAMs; TIGR00682; lpxK; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..395
FT /note="Probable tetraacyldisaccharide 4'-kinase,
FT mitochondrial"
FT /id="PRO_0000421461"
SQ SEQUENCE 395 AA; 44199 MW; B881AB0A789EB247 CRC64;
MEKLRKVVNE IAYTRVHTNS PALHRSLVPF LTIASSLYGV ALQIRRSLYR YSLLQKHRLP
VPVISVGNLS WGGNGKTPMV EYISQFLVDS GLTPLILTRG YAGGDEVKML ERHLRGGPVK
IGVGANRAAT AALFLDKYGC VDSSSLRSFF DLHERAQVWT ISEKIGCIIL DDGMQHWSLS
RDLEIVMLNG LNPWGNGHLM PHGPLREPLL ALERADVAVV HHVDLITKQS LRDIENMIQG
FKKSIPIFYS KMVPKYLFDV KNARSHVALE ALRCASVLCV SAIGSADAFV KSIEMTGAHY
VDRLDFSDHH LFEAEDVETM SRRAKGLEHK SNCKPIIVVT EKDYDRDPEI LKCLDSYTVL
VLCSELQITP ILETDVDSFN YTLMKALAAK FYVSS
