LPXA_ARATH
ID LPXA_ARATH Reviewed; 336 AA.
AC Q9SU91; Q8H1Q9;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial;
DE Short=UDP-N-acetylglucosamine acyltransferase;
DE EC=2.3.1.129;
DE AltName: Full=Protein LIPID X A;
DE Short=AtLpxA;
DE Flags: Precursor;
GN Name=LPXA; OrderedLocusNames=At4g29540; ORFNames=T16L4.50;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 33-336, FUNCTION, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RX PubMed=22545860; DOI=10.1021/bi3002242;
RA Joo S.H., Chung H.S., Raetz C.R., Garrett T.A.;
RT "Activity and crystal structure of Arabidopsis thaliana UDP-N-
RT acetylglucosamine acyltransferase.";
RL Biochemistry 51:4322-4330(2012).
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 (Potential). {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine =
CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-
CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827,
CC ChEBI:CHEBI:173225; EC=2.3.1.129;
CC Evidence={ECO:0000269|PubMed:22545860};
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 1/6. {ECO:0000269|PubMed:21709257}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:22545860}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21709257}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SU91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SU91-2; Sequence=VSP_045743;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants lacking LPXA accumulate very low levels of 2,3-
CC diacylglucosamine-1-phosphate. {ECO:0000269|PubMed:21709257}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000305}.
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DR EMBL; AL079344; CAB45314.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79712.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85641.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85642.1; -; Genomic_DNA.
DR EMBL; AY142528; AAN13071.1; -; mRNA.
DR EMBL; AK175463; BAD43226.1; -; mRNA.
DR PIR; T09917; T09917.
DR RefSeq; NP_001031749.1; NM_001036672.2. [Q9SU91-1]
DR RefSeq; NP_194683.2; NM_119099.3. [Q9SU91-2]
DR PDB; 3T57; X-ray; 2.10 A; A=33-336.
DR PDBsum; 3T57; -.
DR AlphaFoldDB; Q9SU91; -.
DR SMR; Q9SU91; -.
DR BioGRID; 14362; 1.
DR STRING; 3702.AT4G29540.2; -.
DR iPTMnet; Q9SU91; -.
DR PaxDb; Q9SU91; -.
DR PRIDE; Q9SU91; -.
DR EnsemblPlants; AT4G29540.1; AT4G29540.1; AT4G29540. [Q9SU91-2]
DR EnsemblPlants; AT4G29540.2; AT4G29540.2; AT4G29540. [Q9SU91-1]
DR GeneID; 829075; -.
DR Gramene; AT4G29540.1; AT4G29540.1; AT4G29540. [Q9SU91-2]
DR Gramene; AT4G29540.2; AT4G29540.2; AT4G29540. [Q9SU91-1]
DR KEGG; ath:AT4G29540; -.
DR Araport; AT4G29540; -.
DR TAIR; locus:2134368; AT4G29540.
DR eggNOG; ENOG502QRGY; Eukaryota.
DR HOGENOM; CLU_061249_0_0_1; -.
DR InParanoid; Q9SU91; -.
DR OMA; ECVTINR; -.
DR PhylomeDB; Q9SU91; -.
DR BioCyc; ARA:AT4G29540-MON; -.
DR BRENDA; 2.3.1.129; 399.
DR UniPathway; UPA00359; UER00477.
DR PRO; PR:Q9SU91; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU91; baseline and differential.
DR Genevisible; Q9SU91; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IDA: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; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR Gene3D; 1.20.1180.10; -; 1.
DR InterPro; IPR029098; Acetyltransf_C.
DR InterPro; IPR037157; Acetyltransf_C_sf.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR010137; Lipid_A_LpxA.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43480; PTHR43480; 1.
DR Pfam; PF13720; Acetyltransf_11; 1.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..336
FT /note="Probable acyl-[acyl-carrier-protein]--UDP-N-
FT acetylglucosamine O-acyltransferase, mitochondrial"
FT /id="PRO_0000421457"
FT BINDING 128..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 296..297
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_045743"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3T57"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:3T57"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:3T57"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:3T57"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:3T57"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:3T57"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:3T57"
SQ SEQUENCE 336 AA; 36714 MW; D51A40A3FAED226A CRC64;
MISLLKAREK LLSPLVSSTI RRLSSSLSYS REDSRDSEVL IHPSAVVHPN AVIGKGVSVG
PYCTIGSSVK LGNGCKLYPS SHVFGNTELG ESCVLMTGAV VGDELPGYTF IGCNNIIGHH
AVVGVKCQDL KYKHGDECFL CIGNNNEIRE FCSIHRSSKP SDKTVIGDNN LIMGSCHIAH
DCKIGDRNIF ANNTLLAGHV VVEDNTHTAG ASVVHQFCHI GSFAFIGGGS VVSQDVPKYM
MVAGERAELR GLNLEGLRRN GFTMSEMKSL RAAYRKIFMS TETVSLSFEE RLTELEQDQE
LYSVPAVSAM LQSIRDSFTE SRRGICKFRQ WLDSTT
