THIK5_ARATH
ID THIK5_ARATH Reviewed; 457 AA.
AC Q570C8; O65339; Q9S774;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=3-ketoacyl-CoA thiolase 5, peroxisomal;
DE EC=2.3.1.16;
DE AltName: Full=Acetyl-CoA acyltransferase 5;
DE AltName: Full=Beta-ketothiolase 5;
DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase 5;
DE Flags: Precursor;
GN Name=KAT5; OrderedLocusNames=At5g48880; ORFNames=K24G6.22;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia; TISSUE=Aerial part;
RA Ferreira da Rocha P.S.C., Topping J.F., Lindsey K.;
RT "Promoter trapping in Arabidopsis-one T-DNA tag, three transcripts and two
RT thiolase genes.";
RL J. Exp. Bot. 47:S24-S24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-457.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11696182; DOI=10.1046/j.1365-313x.2001.01095.x;
RA Germain V., Rylott E.L., Larson T.R., Sherson S.M., Bechtold N.,
RA Carde J.-P., Bryce J.H., Graham I.A., Smith S.M.;
RT "Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty
RT acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of
RT Arabidopsis seedlings.";
RL Plant J. 28:1-12(2001).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=11891244; DOI=10.1104/pp.010843;
RA He Y., Fukushige H., Hildebrand D.F., Gan S.;
RT "Evidence supporting a role of jasmonic acid in Arabidopsis leaf
RT senescence.";
RL Plant Physiol. 128:876-884(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15141068; DOI=10.1104/pp.104.039925;
RA Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.;
RT "Gene-specific involvement of beta-oxidation in wound-activated responses
RT in Arabidopsis.";
RL Plant Physiol. 135:85-94(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
CC -!- FUNCTION: Probably involved in long chain fatty-acid beta-oxidation
CC prior to gluconeogenesis during germination and subsequent seedling
CC growth. Involved in systemic jasmonic acid (JA) biosynthesis after
CC wounding and may be during senescence. {ECO:0000269|PubMed:11696182,
CC ECO:0000269|PubMed:15141068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PKT2;
CC IsoId=Q570C8-1; Sequence=Displayed;
CC Name=2; Synonyms=PKT1;
CC IsoId=Q570C8-2; Sequence=VSP_015460;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and wounded leaves.
CC {ECO:0000269|PubMed:11696182, ECO:0000269|PubMed:15141068}.
CC -!- DEVELOPMENTAL STAGE: Slightly induced in leaves during senescence.
CC {ECO:0000269|PubMed:11891244}.
CC -!- INDUCTION: Induced by jasmonic acid (JA) and systemically by wounding.
CC Slightly induced by dehydration. {ECO:0000269|PubMed:15141068}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AF062589; AAC17876.1; -; Genomic_DNA.
DR EMBL; AF062589; AAC17877.1; -; Genomic_DNA.
DR EMBL; AF062590; AAC19122.1; -; mRNA.
DR EMBL; AF062591; AAC23571.1; -; mRNA.
DR EMBL; AB012242; BAB09441.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95736.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95737.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95738.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70210.1; -; Genomic_DNA.
DR EMBL; AY079026; AAL84980.1; -; mRNA.
DR EMBL; AY136455; AAM97120.1; -; mRNA.
DR EMBL; BT002594; AAO00954.1; -; mRNA.
DR EMBL; AK220781; BAD94007.1; -; mRNA.
DR PIR; T52165; T52165.
DR RefSeq; NP_001032037.1; NM_001036960.2. [Q570C8-1]
DR RefSeq; NP_001331840.1; NM_001344808.1. [Q570C8-1]
DR RefSeq; NP_568704.2; NM_124265.5. [Q570C8-1]
DR RefSeq; NP_851157.1; NM_180826.4. [Q570C8-2]
DR AlphaFoldDB; Q570C8; -.
DR SMR; Q570C8; -.
DR STRING; 3702.AT5G48880.2; -.
DR iPTMnet; Q570C8; -.
DR PaxDb; Q570C8; -.
DR PRIDE; Q570C8; -.
DR ProteomicsDB; 234366; -. [Q570C8-1]
DR EnsemblPlants; AT5G48880.1; AT5G48880.1; AT5G48880. [Q570C8-2]
DR EnsemblPlants; AT5G48880.2; AT5G48880.2; AT5G48880. [Q570C8-1]
DR EnsemblPlants; AT5G48880.3; AT5G48880.3; AT5G48880. [Q570C8-1]
DR EnsemblPlants; AT5G48880.4; AT5G48880.4; AT5G48880. [Q570C8-1]
DR GeneID; 834946; -.
DR Gramene; AT5G48880.1; AT5G48880.1; AT5G48880. [Q570C8-2]
DR Gramene; AT5G48880.2; AT5G48880.2; AT5G48880. [Q570C8-1]
DR Gramene; AT5G48880.3; AT5G48880.3; AT5G48880. [Q570C8-1]
DR Gramene; AT5G48880.4; AT5G48880.4; AT5G48880. [Q570C8-1]
DR KEGG; ath:AT5G48880; -.
DR Araport; AT5G48880; -.
DR TAIR; locus:2156514; AT5G48880.
DR eggNOG; KOG1389; Eukaryota.
DR InParanoid; Q570C8; -.
DR PhylomeDB; Q570C8; -.
DR BioCyc; ARA:AT5G48880-MON; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q570C8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q570C8; baseline and differential.
DR Genevisible; Q570C8; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Oxylipin biosynthesis; Peroxisome; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..37
FT /note="Peroxisome"
FT /evidence="ECO:0000255"
FT CHAIN 38..457
FT /note="3-ketoacyl-CoA thiolase 5, peroxisomal"
FT /id="PRO_0000034074"
FT ACT_SITE 137
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.1"
FT /id="VSP_015460"
SQ SEQUENCE 457 AA; 47956 MW; 8CF6D8CF80A4DF78 CRC64;
MERAMERQKI LLRHLNPVSS SNSSLKHEPS LLSPVNCVSE VSPMAAFGDD IVIVAAYRTA
ICKARRGGFK DTLPDDLLAS VLKAVVERTS LDPSEVGDIV VGTVIAPGSQ RAMECRVAAY
FAGFPDSVPV RTVNRQCSSG LQAVADVAAS IRAGYYDIGI GAGVESMSTD HIPGGGFHGS
NPRAQDFPKA RDCLLPMGIT SENVAERFGV TREEQDMAAV ESHKRAAAAI ASGKLKDEII
PVATKIVDPE TKAEKAIVVS VDDGVRPNSN MADLAKLKTV FKQNGSTTAG NASQISDGAG
AVLLMKRSLA MKKGLPILGV FRSFAVTGVE PSVMGIGPAV AIPAATKLAG LNVSDIDLFE
INEAFASQYV YSCKKLELDM EKVNVNGGAI AIGHPLGATG ARCVATLLHE MKRRGKDCRF
GVISMCIGTG MGAAAVFERG DSVDNLSNAR VANGDSH
