Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial

Gene

LPXA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).Curated

Catalytic activityi

(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine.1 Publication

Pathwayi: lipid IV(A) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.1 Publication
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial (LPXA)
  2. Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 5 (LPXC5), Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 2 (LPXC2), Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3 (LPXC3), Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 4 (LPXC4), Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1 (LPXC1)
  3. Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial (LPXD2), Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial (LPXD1)
  4. no protein annotated in this organism
  5. Probable lipid-A-disaccharide synthase, mitochondrial (LPXB)
  6. Probable tetraacyldisaccharide 4'-kinase, mitochondrial (LPXK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei199 – 1991SubstrateBy similarity
Binding sitei216 – 2161SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • lipid A biosynthetic process Source: UniProtKB-KW
  • lipid X metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciARA:AT4G29540-MONOMER.
BRENDAi2.3.1.129. 399.
UniPathwayiUPA00359; UER00477.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial (EC:2.3.1.129)
Short name:
UDP-N-acetylglucosamine acyltransferase
Alternative name(s):
Protein LIPID X A
Short name:
AtLpxA
Gene namesi
Name:LPXA
Ordered Locus Names:At4g29540
ORF Names:T16L4.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G29540.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but plants lacking LPXA accumulate very low levels of 2,3-diacylglucosamine-1-phosphate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionSequence analysisAdd
BLAST
Chaini33 – 336304Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrialPRO_0000421457Add
BLAST

Proteomic databases

PaxDbiQ9SU91.
PRIDEiQ9SU91.

PTM databases

iPTMnetiQ9SU91.

Expressioni

Gene expression databases

GenevisibleiQ9SU91. AT.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi14362. 1 interaction.
STRINGi3702.AT4G29540.2.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 473Combined sources
Beta strandi51 – 533Combined sources
Beta strandi69 – 713Combined sources
Beta strandi85 – 895Combined sources
Beta strandi104 – 1118Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi248 – 2525Combined sources
Helixi254 – 2596Combined sources
Helixi264 – 27815Combined sources
Helixi289 – 2979Combined sources
Helixi299 – 3024Combined sources
Helixi305 – 31612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T57X-ray2.10A33-336[»]
ProteinModelPortaliQ9SU91.
SMRiQ9SU91. Positions 40-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni128 – 1314Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IFAW. Eukaryota.
COG1043. LUCA.
HOGENOMiHOG000294326.
InParanoidiQ9SU91.
KOiK00677.
OMAiVQDRSET.
PhylomeDBiQ9SU91.

Family and domain databases

Gene3Di1.20.1180.10. 1 hit.
InterProiIPR029098. Acetyltransf_C.
IPR001451. Hexapep.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9SU91-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MISLLKAREK LLSPLVSSTI RRLSSSLSYS REDSRDSEVL IHPSAVVHPN
60 70 80 90 100
AVIGKGVSVG PYCTIGSSVK LGNGCKLYPS SHVFGNTELG ESCVLMTGAV
110 120 130 140 150
VGDELPGYTF IGCNNIIGHH AVVGVKCQDL KYKHGDECFL CIGNNNEIRE
160 170 180 190 200
FCSIHRSSKP SDKTVIGDNN LIMGSCHIAH DCKIGDRNIF ANNTLLAGHV
210 220 230 240 250
VVEDNTHTAG ASVVHQFCHI GSFAFIGGGS VVSQDVPKYM MVAGERAELR
260 270 280 290 300
GLNLEGLRRN GFTMSEMKSL RAAYRKIFMS TETVSLSFEE RLTELEQDQE
310 320 330
LYSVPAVSAM LQSIRDSFTE SRRGICKFRQ WLDSTT
Length:336
Mass (Da):36,714
Last modified:May 1, 2000 - v1
Checksum:iD51A40A3FAED226A
GO
Isoform 2 (identifier: Q9SU91-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     296-297: Missing.

Note: No experimental confirmation available.
Show »
Length:334
Mass (Da):36,457
Checksum:i54D00E5E8024B329
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 2972Missing in isoform 2. 1 PublicationVSP_045743

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL079344 Genomic DNA. Translation: CAB45314.1.
AL161575 Genomic DNA. Translation: CAB79712.1.
CP002687 Genomic DNA. Translation: AEE85641.1.
CP002687 Genomic DNA. Translation: AEE85642.1.
AY142528 mRNA. Translation: AAN13071.1.
AK175463 mRNA. Translation: BAD43226.1.
PIRiT09917.
RefSeqiNP_001031749.1. NM_001036672.1. [Q9SU91-1]
NP_194683.2. NM_119099.3. [Q9SU91-2]
UniGeneiAt.31911.

Genome annotation databases

EnsemblPlantsiAT4G29540.2; AT4G29540.2; AT4G29540. [Q9SU91-1]
GeneIDi829075.
KEGGiath:AT4G29540.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL079344 Genomic DNA. Translation: CAB45314.1.
AL161575 Genomic DNA. Translation: CAB79712.1.
CP002687 Genomic DNA. Translation: AEE85641.1.
CP002687 Genomic DNA. Translation: AEE85642.1.
AY142528 mRNA. Translation: AAN13071.1.
AK175463 mRNA. Translation: BAD43226.1.
PIRiT09917.
RefSeqiNP_001031749.1. NM_001036672.1. [Q9SU91-1]
NP_194683.2. NM_119099.3. [Q9SU91-2]
UniGeneiAt.31911.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T57X-ray2.10A33-336[»]
ProteinModelPortaliQ9SU91.
SMRiQ9SU91. Positions 40-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14362. 1 interaction.
STRINGi3702.AT4G29540.2.

PTM databases

iPTMnetiQ9SU91.

Proteomic databases

PaxDbiQ9SU91.
PRIDEiQ9SU91.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G29540.2; AT4G29540.2; AT4G29540. [Q9SU91-1]
GeneIDi829075.
KEGGiath:AT4G29540.

Organism-specific databases

TAIRiAT4G29540.

Phylogenomic databases

eggNOGiENOG410IFAW. Eukaryota.
COG1043. LUCA.
HOGENOMiHOG000294326.
InParanoidiQ9SU91.
KOiK00677.
OMAiVQDRSET.
PhylomeDBiQ9SU91.

Enzyme and pathway databases

UniPathwayiUPA00359; UER00477.
BioCyciARA:AT4G29540-MONOMER.
BRENDAi2.3.1.129. 399.

Miscellaneous databases

PROiQ9SU91.

Gene expression databases

GenevisibleiQ9SU91. AT.

Family and domain databases

Gene3Di1.20.1180.10. 1 hit.
InterProiIPR029098. Acetyltransf_C.
IPR001451. Hexapep.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  5. "Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that of Escherichia coli."
    Li C., Guan Z., Liu D., Raetz C.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:11387-11392(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PATHWAY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE, DISRUPTION PHENOTYPE.
  6. "Activity and crystal structure of Arabidopsis thaliana UDP-N-acetylglucosamine acyltransferase."
    Joo S.H., Chung H.S., Raetz C.R., Garrett T.A.
    Biochemistry 51:4322-4330(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 33-336, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.

Entry informationi

Entry nameiLPXA_ARATH
AccessioniPrimary (citable) accession number: Q9SU91
Secondary accession number(s): Q8H1Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: May 1, 2000
Last modified: January 20, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.