THIK1_ARATH
ID THIK1_ARATH Reviewed; 443 AA.
AC Q8LF48; O23014; Q8LPI4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=3-ketoacyl-CoA thiolase 1, peroxisomal;
DE EC=2.3.1.16;
DE AltName: Full=Acetyl-CoA acyltransferase 1;
DE AltName: Full=Beta-ketothiolase 1;
DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase 1;
DE Flags: Precursor;
GN Name=KAT1; OrderedLocusNames=At1g04710; ORFNames=T1G11.4;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
RP TISSUE SPECIFICITY.
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 [7]
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: Involved in fatty-acid beta-oxidation prior to
CC gluconeogenesis during germination and subsequent seedling growth.
CC Implicated in jasmonic acid (JA) biosynthesis (By similarity).
CC {ECO:0000250}.
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 -!- INTERACTION:
CC Q8LF48; Q9XF57: PEX7; NbExp=3; IntAct=EBI-25521360, EBI-9536794;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Low levels in seedlings and leaves.
CC {ECO:0000269|PubMed:11696182, ECO:0000269|PubMed:15141068}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002376; AAB80634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27736.1; -; Genomic_DNA.
DR EMBL; AY099741; AAM20592.1; -; mRNA.
DR EMBL; BT003415; AAO30078.1; -; mRNA.
DR EMBL; AY085052; AAM61609.1; -; mRNA.
DR PIR; A86180; A86180.
DR RefSeq; NP_171965.1; NM_100351.5.
DR AlphaFoldDB; Q8LF48; -.
DR SMR; Q8LF48; -.
DR BioGRID; 24669; 1.
DR IntAct; Q8LF48; 1.
DR STRING; 3702.AT1G04710.1; -.
DR iPTMnet; Q8LF48; -.
DR PaxDb; Q8LF48; -.
DR PRIDE; Q8LF48; -.
DR ProteomicsDB; 234392; -.
DR EnsemblPlants; AT1G04710.1; AT1G04710.1; AT1G04710.
DR GeneID; 839434; -.
DR Gramene; AT1G04710.1; AT1G04710.1; AT1G04710.
DR KEGG; ath:AT1G04710; -.
DR Araport; AT1G04710; -.
DR TAIR; locus:2197778; AT1G04710.
DR eggNOG; KOG1389; Eukaryota.
DR HOGENOM; CLU_031026_1_1_1; -.
DR OMA; AVNRHCA; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; Q8LF48; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q8LF48; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LF48; baseline and differential.
DR Genevisible; Q8LF48; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; 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 PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 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; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Oxylipin biosynthesis; Peroxisome;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..30
FT /note="Peroxisome"
FT /evidence="ECO:0000255"
FT CHAIN 31..443
FT /note="3-ketoacyl-CoA thiolase 1, peroxisomal"
FT /id="PRO_0000034072"
FT ACT_SITE 130
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT CONFLICT 369
FT /note="L -> Q (in Ref. 4; AAM61609)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="G -> D (in Ref. 4; AAM61609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 46611 MW; B04112889A16E704 CRC64;
MEKATERQRI LLRHLQPSSS SDASLSASAC LSKDSAAYQY GDDVVIVAAQ RTALCKAKRG
SFKDTFPDEL LASVLRALIE KTNVNPSEVG DIVVGTVLGP GSQRASECRM AAFYAGFPET
VPIRTVNRQC SSGLQAVADV AAAIKAGFYD IGIGAGLESM TTNPRGWKGS VNPNVKKFEQ
AHNCLLPMGI TSENVAHRFN VSREEQDQAA VDSHRKAASA TASGKFKDEI TPVKTKIVDP
KTGDEKPITV SVDDGIRPNT TLSGLAKLKP VFKEDGTTTA GNSSQLSDGA GAVLLMRRNV
AMQKGLPILG VFRTFSAVGV DPAIMGVGPA VAIPAAVKAA GLELNDVDLF EINEAFASQF
VYCRNKLGLD AEKINVNGGA IAIGHPLGAT GARCVATLLH EMKRRGKDCR FGVVSMCIGS
GMGAAAVFER GGGVDELCDV RKV
