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Protein

3-ketoacyl-CoA thiolase 2, peroxisomal

Gene

PED1

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

Functioni

Involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Confers sensitivity to 2,4-dichlorophenoxybutiric acid (2,4-DB). Required for local and systemic induction of jasmonic acid (JA) biosynthesis after wounding. Seems to be involved in JA biosynthesis during senescence.5 Publications

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Kineticsi

  1. KM=77.5 µM for acetoacetyl-CoA (at 25 degrees Celsius)1 Publication
  1. Vmax=5000 nmol/min/mg enzyme (at 25 degrees Celsius)1 Publication

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei138Acyl-thioester intermediateBy similarity1
Active sitei393Proton acceptorPROSITE-ProRule annotation1
Active sitei425Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • acetyl-CoA C-acyltransferase activity Source: TAIR

GO - Biological processi

  • fatty acid beta-oxidation Source: TAIR
  • fatty acid biosynthetic process Source: UniProtKB-KW
  • glyoxysome organization Source: TAIR
  • jasmonic acid biosynthetic process Source: TAIR
  • oxylipin biosynthetic process Source: UniProtKB-KW
  • positive regulation of abscisic acid-activated signaling pathway Source: TAIR
  • response to wounding Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:AT2G33150-MONOMER.
BRENDAi2.3.1.16. 399.
ReactomeiR-ATH-2046106. alpha-linolenic acid (ALA) metabolism.
R-ATH-390247. Beta-oxidation of very long chain fatty acids.
R-ATH-6798695. Neutrophil degranulation.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase 2, peroxisomal (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase 2
Beta-ketothiolase 2
Peroxisomal 3-oxoacyl-CoA thiolase 2
Peroxisome defective protein 1
Gene namesi
Name:PED1
Synonyms:KAT2
Ordered Locus Names:At2g33150
ORF Names:F25I18.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G33150.

Subcellular locationi

  • Peroxisome
  • Glyoxysome

  • Note: Peroxisomal targeting signal type 2 (PTS2-type) import is temperature and ATP-dependent, induced by zinc ions and PTS1-type import, but repressed by mature forms of PED1.

GO - Cellular componenti

  • chloroplast Source: TAIR
  • glyoxysome Source: UniProtKB-SubCell
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • nucleolus Source: TAIR
  • peroxisome Source: TAIR
  • vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34PeroxisomeSequence analysisAdd BLAST34
ChainiPRO_000003407335 – 4623-ketoacyl-CoA thiolase 2, peroxisomalAdd BLAST428

Proteomic databases

PaxDbiQ56WD9.
PRIDEiQ56WD9.

Expressioni

Tissue specificityi

Accumulates in etiolated cotyledons and in seedlings, also present in roots, flowers and siliques (at protein level). High levels in wounded leaves.4 Publications

Developmental stagei

Levels increase strongly upon imbibition and decrease 3 days later. Strongly induced in leaves during senescence.3 Publications

Inductioni

Expressed in the dark, repressed by light (at protein level). Induced by dehydration, by abscisic acid (ABA) and by wounding, both locally and systemically.3 Publications

Gene expression databases

GenevisibleiQ56WD9. AT.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi3223. 5 interactors.
IntActiQ56WD9. 3 interactors.
MINTiMINT-8059930.
STRINGi3702.AT2G33150.1.

Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 47Combined sources7
Helixi48 – 50Combined sources3
Beta strandi52 – 59Combined sources8
Turni65 – 67Combined sources3
Turni69 – 72Combined sources4
Helixi75 – 90Combined sources16
Helixi94 – 96Combined sources3
Beta strandi100 – 103Combined sources4
Beta strandi106 – 108Combined sources3
Helixi109 – 122Combined sources14
Beta strandi131 – 135Combined sources5
Helixi137 – 139Combined sources3
Helixi140 – 153Combined sources14
Beta strandi158 – 167Combined sources10
Turni168 – 170Combined sources3
Helixi181 – 185Combined sources5
Helixi187 – 191Combined sources5
Helixi196 – 207Combined sources12
Helixi211 – 230Combined sources20
Turni231 – 237Combined sources7
Beta strandi241 – 246Combined sources6
Turni248 – 250Combined sources3
Beta strandi253 – 258Combined sources6
Helixi270 – 274Combined sources5
Beta strandi279 – 281Combined sources3
Helixi288 – 290Combined sources3
Beta strandi295 – 305Combined sources11
Helixi306 – 312Combined sources7
Beta strandi318 – 327Combined sources10
Helixi330 – 335Combined sources6
Helixi336 – 347Combined sources12
Helixi352 – 354Combined sources3
Beta strandi357 – 360Combined sources4
Helixi365 – 375Combined sources11
Helixi379 – 381Combined sources3
Helixi388 – 391Combined sources4
Helixi397 – 413Combined sources17
Beta strandi419 – 426Combined sources8
Turni427 – 429Combined sources3
Beta strandi430 – 438Combined sources9
Helixi441 – 446Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C7YX-ray2.10A/B38-441[»]
2C7ZX-ray2.37A38-441[»]
2WU9X-ray1.50A/B36-462[»]
ProteinModelPortaliQ56WD9.
SMRiQ56WD9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56WD9.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1389. Eukaryota.
COG0183. LUCA.
HOGENOMiHOG000012239.
InParanoidiQ56WD9.
KOiK07513.
OMAiPQGKEDG.
OrthoDBiEOG09360EBQ.
PhylomeDBiQ56WD9.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q56WD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKAIERQRV LLEHLRPSSS SSHNYEASLS ASACLAGDSA AYQRTSLYGD
60 70 80 90 100
DVVIVAAHRT PLCKSKRGNF KDTYPDDLLA PVLRALIEKT NLNPSEVGDI
110 120 130 140 150
VVGTVLAPGS QRASECRMAA FYAGFPETVA VRTVNRQCSS GLQAVADVAA
160 170 180 190 200
AIKAGFYDIG IGAGLESMTT NPMAWEGSVN PAVKKFAQAQ NCLLPMGVTS
210 220 230 240 250
ENVAQRFGVS RQEQDQAAVD SHRKAAAATA AGKFKDEIIP VKTKLVDPKT
260 270 280 290 300
GDEKPITVSV DDGIRPTTTL ASLGKLKPVF KKDGTTTAGN SSQVSDGAGA
310 320 330 340 350
VLLMKRSVAM QKGLPVLGVF RTFAAVGVDP AIMGIGPAVA IPAAVKAAGL
360 370 380 390 400
ELDDIDLFEI NEAFASQFVY CRNKLGLDPE KINVNGGAMA IGHPLGATGA
410 420 430 440 450
RCVATLLHEM KRRGKDCRFG VVSMCIGTGM GAAAVFERGD GVDELRNARK
460
VEAQGLLSKD AR
Length:462
Mass (Da):48,579
Last modified:August 30, 2005 - v2
Checksum:i7405F81968489ADB
GO

Sequence cautioni

The sequence AAL25590 differs from that shown. Reason: Frameshift at position 375.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17P → F (PubMed:14630959).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008854 mRNA. Translation: BAA25248.1.
AB008855 Genomic DNA. Translation: BAA25249.1.
AC002334 Genomic DNA. Translation: AAC04908.1.
CP002685 Genomic DNA. Translation: AEC08791.1.
AY058176 mRNA. Translation: AAL25590.1. Frameshift.
AF327529 mRNA. Translation: AAG42910.1.
AF349530 mRNA. Translation: AAK15577.1.
AY052702 mRNA. Translation: AAK96606.1.
AY063720 mRNA. Translation: AAL36070.1.
AY087543 mRNA. Translation: AAM65085.1.
AK222103 mRNA. Translation: BAD95031.1.
PIRiT52110.
RefSeqiNP_180873.1. NM_128874.4.
UniGeneiAt.23661.
At.72951.

Genome annotation databases

EnsemblPlantsiAT2G33150.1; AT2G33150.1; AT2G33150.
GeneIDi817876.
GrameneiAT2G33150.1; AT2G33150.1; AT2G33150.
KEGGiath:AT2G33150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008854 mRNA. Translation: BAA25248.1.
AB008855 Genomic DNA. Translation: BAA25249.1.
AC002334 Genomic DNA. Translation: AAC04908.1.
CP002685 Genomic DNA. Translation: AEC08791.1.
AY058176 mRNA. Translation: AAL25590.1. Frameshift.
AF327529 mRNA. Translation: AAG42910.1.
AF349530 mRNA. Translation: AAK15577.1.
AY052702 mRNA. Translation: AAK96606.1.
AY063720 mRNA. Translation: AAL36070.1.
AY087543 mRNA. Translation: AAM65085.1.
AK222103 mRNA. Translation: BAD95031.1.
PIRiT52110.
RefSeqiNP_180873.1. NM_128874.4.
UniGeneiAt.23661.
At.72951.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C7YX-ray2.10A/B38-441[»]
2C7ZX-ray2.37A38-441[»]
2WU9X-ray1.50A/B36-462[»]
ProteinModelPortaliQ56WD9.
SMRiQ56WD9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3223. 5 interactors.
IntActiQ56WD9. 3 interactors.
MINTiMINT-8059930.
STRINGi3702.AT2G33150.1.

Proteomic databases

PaxDbiQ56WD9.
PRIDEiQ56WD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G33150.1; AT2G33150.1; AT2G33150.
GeneIDi817876.
GrameneiAT2G33150.1; AT2G33150.1; AT2G33150.
KEGGiath:AT2G33150.

Organism-specific databases

TAIRiAT2G33150.

Phylogenomic databases

eggNOGiKOG1389. Eukaryota.
COG0183. LUCA.
HOGENOMiHOG000012239.
InParanoidiQ56WD9.
KOiK07513.
OMAiPQGKEDG.
OrthoDBiEOG09360EBQ.
PhylomeDBiQ56WD9.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciMetaCyc:AT2G33150-MONOMER.
BRENDAi2.3.1.16. 399.
ReactomeiR-ATH-2046106. alpha-linolenic acid (ALA) metabolism.
R-ATH-390247. Beta-oxidation of very long chain fatty acids.
R-ATH-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiQ56WD9.
PROiQ56WD9.

Gene expression databases

GenevisibleiQ56WD9. AT.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIK2_ARATH
AccessioniPrimary (citable) accession number: Q56WD9
Secondary accession number(s): Q93Z35, Q9S7M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: November 30, 2016
This is version 102 of the entry and version 2 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.