LPXD2_ARATH
ID LPXD2_ARATH Reviewed; 304 AA.
AC F4JIP6; O49563;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial {ECO:0000303|PubMed:21709257};
DE EC=2.3.1.- {ECO:0000303|PubMed:21709257};
DE AltName: Full=Protein LIPID X D2;
DE Short=AtLpxD2;
DE Flags: Precursor;
GN Name=LPXD2; OrderedLocusNames=At4g21220; ORFNames=F7J7.160;
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:0000303|PubMed:21709257}.
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 -!- 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 LPXD2 do not accumulate 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=CAA17541.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79122.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021960; CAA17541.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79122.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84429.1; -; Genomic_DNA.
DR PIR; T04953; T04953.
DR RefSeq; NP_193854.2; NM_118241.3.
DR AlphaFoldDB; F4JIP6; -.
DR SMR; F4JIP6; -.
DR STRING; 3702.AT4G21220.1; -.
DR PaxDb; F4JIP6; -.
DR PRIDE; F4JIP6; -.
DR ProteomicsDB; 238728; -.
DR EnsemblPlants; AT4G21220.1; AT4G21220.1; AT4G21220.
DR GeneID; 827871; -.
DR Gramene; AT4G21220.1; AT4G21220.1; AT4G21220.
DR KEGG; ath:AT4G21220; -.
DR Araport; AT4G21220; -.
DR TAIR; locus:2127423; AT4G21220.
DR eggNOG; ENOG502QV70; Eukaryota.
DR HOGENOM; CLU_049865_3_2_1; -.
DR InParanoid; F4JIP6; -.
DR OMA; YKIPHAG; -.
DR OrthoDB; 1270774at2759; -.
DR UniPathway; UPA00359; UER00479.
DR PRO; PR:F4JIP6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JIP6; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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:TAIR.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001289; P:lipid X metabolic process; IMP:TAIR.
DR CDD; cd03352; LbH_LpxD; 1.
DR InterPro; IPR001451; Hexapep.
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 TIGRFAMs; TIGR01853; lipid_A_lpxD; 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..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..304
FT /note="Probable UDP-3-O-acylglucosamine N-acyltransferase
FT 2, mitochondrial"
FT /id="PRO_0000421459"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 159..161
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 253
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 304 AA; 32331 MW; 6CBC69967C4221E9 CRC64;
MAATLWRLYS KSICNSLQGI ILNKPFIQKQ LLLSSRTRSL SFSSDSQFGS ATAEVCSNTG
LKTGGGIIVK EGFLRWENGG GTCHSSAQIY SSALVEFGAV VHEKAVLGAE VHVGSGTVIG
PSVDIGPSTR IGYNVSISNC SIGDSCVIHN GVCIGQDGFG FYVDEHGNMV KKPQTLNVKI
GNRVEIGANT CIDRGSWRET VIEDDTKIDN LVQIGHNVII GKCCLLCGQV GIAGSVTIGD
YVALGGRAAV RDHVSIVSKV RLAANSCVTR NITEPGDFGG FPAVPIHEWR KQIVRAQIAN
KREI
