LPXD1_ARATH
ID LPXD1_ARATH Reviewed; 330 AA.
AC F4JGP6; Q9M0X4;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial;
DE EC=2.3.1.191;
DE AltName: Full=Protein LIPID X D1;
DE Short=AtLpxD1;
DE Flags: Precursor;
GN Name=LPXD1; OrderedLocusNames=At4g05210; ORFNames=C17L7.130;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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. Lipid A-like molecules in plants may serve as
CC structural components of the outer membranes of mitochondria and/or
CC chloroplasts, or may be involved in signal transduction or plant
CC defense responses. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-
CC alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC EC=2.3.1.191;
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 3/6. {ECO:0000269|PubMed:21709257}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21709257}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants lacking LPXD1 accumulate very low levels of 2,3-
CC diacylglucosamine-1-phosphate. {ECO:0000269|PubMed:21709257}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81063.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161503; CAB81063.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82491.1; -; Genomic_DNA.
DR PIR; E85065; E85065.
DR RefSeq; NP_192430.2; NM_116760.2.
DR AlphaFoldDB; F4JGP6; -.
DR SMR; F4JGP6; -.
DR STRING; 3702.AT4G05210.1; -.
DR PaxDb; F4JGP6; -.
DR PRIDE; F4JGP6; -.
DR EnsemblPlants; AT4G05210.1; AT4G05210.1; AT4G05210.
DR GeneID; 825869; -.
DR Gramene; AT4G05210.1; AT4G05210.1; AT4G05210.
DR KEGG; ath:AT4G05210; -.
DR Araport; AT4G05210; -.
DR TAIR; locus:2115743; AT4G05210.
DR eggNOG; ENOG502QV70; Eukaryota.
DR HOGENOM; CLU_049865_3_2_1; -.
DR InParanoid; F4JGP6; -.
DR OrthoDB; 1270774at2759; -.
DR BRENDA; 2.3.1.191; 399.
DR UniPathway; UPA00359; UER00479.
DR PRO; PR:F4JGP6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JGP6; baseline and differential.
DR Genevisible; F4JGP6; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase 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 CDD; cd03352; LbH_LpxD; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR007691; LpxD.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43378; PTHR43378; 1.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..330
FT /note="Probable UDP-3-O-acylglucosamine N-acyltransferase
FT 1, mitochondrial"
FT /id="PRO_0000421458"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 160..162
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT SITE 9
FT /note="Participates in a stacking interaction with the
FT uracil ring of UDP-GlcNAc"
FT /evidence="ECO:0000250"
SQ SEQUENCE 330 AA; 35708 MW; FCDFFBCBA8C3D00C CRC64;
MANSLRTLFS VSTHGVFLNK RSSYRVRKVF VGMPLRICSE IPRFVSVSCI RSDMCGIMML
GKDVHDLLET SSGGNVEKGF LRWRNGGGMY HRSALIDSSA LVEFGAVVHQ EAILGAEVHI
GSNTVIGSSV KIGPSTKIGN CSIGDLCVIH NGVCIGQDGF GFYVDDNGNM VKKPQTLNVK
IGNRVEIGAN TCIDRGSWRD TVIGDDTKID NLVQIGHNVI IGKCCLFCGQ VGIAGSAEIG
DFVALGGRVA VRDHVSIVSK VRLAANSCVT KNITEPGDYG GFPAYKKTEP DSAFASDKHC
FILQKILIQV PIHQWRRQIV EAQISSKRKP
