ID THIK_HUMAN Reviewed; 424 AA. AC P09110; G5E935; Q96CA6; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 02-SEP-2026, entry version 241. DE RecName: Full=3-ketoacyl-CoA thiolase, peroxisomal {ECO:0000305}; DE EC=2.3.1.16 {ECO:0000305|PubMed:2882519}; DE AltName: Full=Acetyl-CoA C-myristoyltransferase; DE EC=2.3.1.155 {ECO:0000305|PubMed:2882519}; DE AltName: Full=Acetyl-CoA acyltransferase; DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P21775}; DE AltName: Full=Beta-ketothiolase; DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase {ECO:0000303|PubMed:2882519}; DE Flags: Precursor; GN Name=ACAA1 {ECO:0000312|HGNC:HGNC:82}; Synonyms=ACAA, PTHIO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=3194209; DOI=10.1093/nar/16.21.10369; RA Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.; RT "Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase."; RL Nucleic Acids Res. 16:10369-10369(1988). RN [2] RP SEQUENCE REVISION TO 285-287. RA Bout A.; RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=2726492; DOI=10.1093/nar/17.9.3588; RA Fairbairn L.J., Tanner M.J.A.; RT "Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA RT thiolase."; RL Nucleic Acids Res. 17:3588-3588(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1679347; DOI=10.1016/0167-4781(91)90035-k; RA Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.; RT "Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA RT thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient RT patient."; RL Biochim. Biophys. Acta 1090:43-51(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP ALA-387. RC TISSUE=Lymph, Ovary, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=2882519; DOI=10.1073/pnas.84.8.2494; RA Schram A.W., Goldfischer S., van Roermund C.W., Brouwer-Kelder E.M., RA Collins J., Hashimoto T., Heymans H.S., van den Bosch H., Schutgens R.B., RA Tager J.M.; RT "Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency."; RL Proc. Natl. Acad. Sci. U.S.A. 84:2494-2496(1987). RN [9] RP REVIEW ON BIOCHEMICAL CHARACTERISTICS OF THE PEROXISOMAL DISORDERS, AND RP FUNCTION. RX PubMed=7685190; DOI=10.1016/0300-9084(93)90087-9; RA Wanders R.J., Schutgens R.B., Barth P.G., Tager J.M., van den Bosch H.; RT "Postnatal diagnosis of peroxisomal disorders: a biochemical approach."; RL Biochimie 75:269-279(1993). RN [10] RP REVIEW ON POSSIBLE BIOSYNTHESIS PATHWAYS OF PUFAS, FUNCTION, AND CAUTION. RX PubMed=10903473; DOI=10.1016/s1388-1981(00)00077-9; RA Sprecher H.; RT "Metabolism of highly unsaturated n-3 and n-6 fatty acids."; RL Biochim. Biophys. Acta 1486:219-231(2000). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=11734571; DOI=10.1016/s0022-2275(20)31527-3; RA Ferdinandusse S., Denis S., Mooijer P.A., Zhang Z., Reddy J.K., RA Spector A.A., Wanders R.J.; RT "Identification of the peroxisomal beta-oxidation enzymes involved in the RT biosynthesis of docosahexaenoic acid."; RL J. Lipid Res. 42:1987-1995(2001). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND THR-60, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP SUBCELLULAR LOCATION, INTERACTION WITH PEX7, AND MUTAGENESIS OF GLN-5; RP VAL-6; VAL-7; LEU-8; GLY-9 AND HIS-10. RX PubMed=22057399; DOI=10.1074/jbc.m111.301853; RA Kunze M., Neuberger G., Maurer-Stroh S., Ma J., Eck T., Braverman N., RA Schmid J.A., Eisenhaber F., Berger J.; RT "Structural requirements for interaction of peroxisomal targeting signal 2 RT and its receptor PEX7."; RL J. Biol. Chem. 286:45048-45062(2011). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-26, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH PEX7. RX PubMed=25538232; DOI=10.1074/jbc.m114.601575; RA Kunze M., Malkani N., Maurer-Stroh S., Wiesinger C., Schmid J.A., RA Berger J.; RT "Mechanistic insights into PTS2-mediated peroxisomal protein import: the RT co-receptor PEX5L drastically increases the interaction strength between RT the cargo protein and the receptor PEX7."; RL J. Biol. Chem. 290:4928-4940(2015). RN [18] RP REVIEW ON THE PHYSIOLOGICAL ROLE OF THE PEROXISOMAL FATTY ACID RP BETA-OXIDATION, FUNCTION, AND CAUTION. RX PubMed=35951481; DOI=10.1152/physrev.00051.2021; RA Wanders R.J.A., Baes M., Ribeiro D., Ferdinandusse S., Waterham H.R.; RT "The physiological functions of human peroxisomes."; RL Physiol. Rev. 103:957-1024(2023). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, AND SUBUNIT. RG Structural genomics consortium (SGC); RT "Crystal structure of human peroxisomal acetyl-COA acyl transferase 1 RT (ACAA1)."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Responsible for the thiolytic cleavage of straight chain 3- CC keto fatty acyl-CoAs (3-oxoacyl-CoAs) (PubMed:11734571, CC PubMed:2882519). Plays an important role in fatty acid peroxisomal CC beta-oxidation (PubMed:11734571, PubMed:2882519). Catalyzes the CC cleavage of medium, long, and very long straight chain 3-oxoacyl-CoAs CC (PubMed:11734571, PubMed:2882519). May play a role in peroxisomal beta- CC oxidation step in polyunsaturated fatty acids (PUFAs) biosynthesis. CC Possibly regulates systemic levels of docosahexaenoic acid (DHA, CC C22:6n-3) through a process involving endoplasmic reticulum CC desaturation and elongation of alpha-linolenic acid (ALA, C18:3n-3) to CC form tetracosahexaenoic acid (THA, C24:6n-3), which is then beta- CC oxidized to DHA in peroxisomes. {ECO:0000303|PubMed:10903473, CC ECO:0000303|PubMed:35951481, ECO:0000303|PubMed:7685190, CC ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519, CC ECO:0000305|PubMed:35951481}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an acyl-CoA + acetyl-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 Evidence={ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; CC Evidence={ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a very long-chain fatty acyl-CoA + acetyl-CoA = a very-long- CC chain 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:78895, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:90725, ChEBI:CHEBI:138261; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78897; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octacosanoyl-CoA + acetyl-CoA = 3-oxo-triacontanoyl-CoA + CoA; CC Xref=Rhea:RHEA:85327, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:74141, ChEBI:CHEBI:74228; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:85329; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexacosanoyl-CoA + acetyl-CoA = 3-oxooctacosanyol-CoA + CoA; CC Xref=Rhea:RHEA:85331, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:64868, ChEBI:CHEBI:73976; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:85333; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetracosanoyl-CoA + acetyl-CoA = 3-oxohexacosanoyl-CoA + CoA; CC Xref=Rhea:RHEA:78639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:65052, ChEBI:CHEBI:73980; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78641; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=docosanoyl-CoA + acetyl-CoA = 3-oxotetracosanoyl-CoA + CoA; CC Xref=Rhea:RHEA:78567, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:65059, ChEBI:CHEBI:73977; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78569; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(17Z)-hexacosenoyl-CoA + CoA = (15Z)-tetracosenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83127, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:74128, ChEBI:CHEBI:232759; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83128; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(15Z)-tetracosenoyl-CoA + CoA = (13Z)-docosenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83083, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:74068, ChEBI:CHEBI:74071; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83084; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + CoA = CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + acetyl-CoA; CC Xref=Rhea:RHEA:39131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:74298, ChEBI:CHEBI:74304; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39132; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(6Z,9Z,12Z,15Z,18Z)-tetracosapentaenoyl-CoA + CoA = CC (4Z,7Z,10Z,13Z,16Z)-docosapentaenoyl-CoA + acetyl-CoA; CC Xref=Rhea:RHEA:39147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:76367, ChEBI:CHEBI:76368; CC Evidence={ECO:0000305|PubMed:11734571}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39148; CC Evidence={ECO:0000305|PubMed:11734571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a long-chain fatty acyl-CoA + acetyl-CoA = a long-chain 3-oxo- CC fatty acyl-CoA + CoA; Xref=Rhea:RHEA:78899, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:83139, ChEBI:CHEBI:136758; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78901; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=eicosanoyl-CoA + acetyl-CoA = 3-oxodocosanoyl-CoA + CoA; CC Xref=Rhea:RHEA:78583, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57380, ChEBI:CHEBI:71451; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78585; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octadecanoyl-CoA + acetyl-CoA = 3-oxoeicosanoyl-CoA + CoA; CC Xref=Rhea:RHEA:78599, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65115; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78601; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanoyl-CoA + acetyl-CoA = 3-oxooctadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:71407; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetradecanoyl-CoA + acetyl-CoA = 3-oxohexadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + acetyl-CoA = 3-oxotetradecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(13Z)-docosenoyl-CoA + CoA = (11Z)-eicosenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83095, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:74069, ChEBI:CHEBI:74070; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83096; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(11Z)-eicosenoyl-CoA + CoA = (9Z)-octadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83099, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83100; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(7Z-hexadecenoyl)-CoA + CoA = (5Z)-tetradecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:47444, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:84650, ChEBI:CHEBI:87719; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47445; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(5Z-tetradecenoyl)-CoA + CoA = (3Z)-dodecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:47460, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58543, ChEBI:CHEBI:87707; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47461; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(11Z)-docosenoyl-CoA + CoA = (9Z)-eicosenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83331, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:232890, ChEBI:CHEBI:232891; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83332; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(9Z)-eicosenoyl-CoA + CoA = (7Z)-octadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83367, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:152050, ChEBI:CHEBI:232898; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83368; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(7Z)-octadecenoyl-CoA + CoA = (5Z)-hexadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83383, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:232901, ChEBI:CHEBI:232908; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83384; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(5Z)-hexadecenoyl-CoA + CoA = (3Z)-tetradecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:83399, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61968, ChEBI:CHEBI:232912; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83400; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CoA = CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + acetyl-CoA; CC Xref=Rhea:RHEA:84391, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57368, ChEBI:CHEBI:73852; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84392; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + CoA = CC (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + acetyl-CoA; CC Xref=Rhea:RHEA:84311, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:73862, ChEBI:CHEBI:73863; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84312; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(8Z,11Z,14Z)-eicosatrienoyl-CoA + CoA = (6Z,9Z,12Z)- CC octadecatrienoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:84903, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57363, CC ChEBI:CHEBI:71481; Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84904; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + CoA = CC (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + acetyl-CoA; CC Xref=Rhea:RHEA:84835, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:71489, ChEBI:CHEBI:71491; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84836; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(6Z,9Z,12Z)-octadecatrienoyl-CoA + CoA = (4Z,7Z,10Z)- CC hexadecatrienoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:84715, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:233780, CC ChEBI:CHEBI:233781; Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84716; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + CoA = CC (4Z,7Z,10Z,13Z)-hexadecatetraenoyl-CoA + acetyl-CoA; CC Xref=Rhea:RHEA:84839, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:233746, ChEBI:CHEBI:233765; CC Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84840; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(7Z,10Z)-hexadecadienoyl-CoA + CoA = (5Z,8Z)- CC tetradecadienoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:84451, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:233788, CC ChEBI:CHEBI:233789; Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84452; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(7Z,10Z,13Z)-hexadecatrienoyl-CoA + CoA = (5Z,8Z,11Z)- CC tetradecatrienoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:84699, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:233794, CC ChEBI:CHEBI:233795; Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84700; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(8Z,11Z)-tetradecadienoyl-CoA + CoA = (6Z,9Z)- CC dodecadienoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:84703, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:233803, CC ChEBI:CHEBI:233810; Evidence={ECO:0000305|PubMed:2882519}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84704; CC Evidence={ECO:0000305|PubMed:2882519}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a medium-chain fatty acyl-CoA + acetyl-CoA = a medium-chain 3- CC oxoacyl-CoA + CoA; Xref=Rhea:RHEA:78903, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:90546, ChEBI:CHEBI:229604; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:78905; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanoyl-CoA + acetyl-CoA = 3-oxododecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octanoyl-CoA + acetyl-CoA = 3-oxodecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexanoyl-CoA + acetyl-CoA = 3-oxooctanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxohexadecanedioyl-CoA + CoA = tetradecanedioyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344; CC Evidence={ECO:0000250|UniProtKB:P21775}; CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. CC {ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519}. CC -!- SUBUNIT: Homodimer (Ref.19). Interacts (via PTS2-type peroxisomal CC targeting signal region) with PEX7; leading to its translocation into CC peroxisomes (PubMed:22057399, PubMed:25538232). CC {ECO:0000269|PubMed:22057399, ECO:0000269|PubMed:25538232, CC ECO:0000269|Ref.19}. CC -!- INTERACTION: CC P09110; Q9BSK4: FEM1A; NbExp=3; IntAct=EBI-3926709, EBI-2515349; CC P09110; Q12800: TFCP2; NbExp=3; IntAct=EBI-3926709, EBI-717422; CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:22057399, CC ECO:0000269|PubMed:25538232}. Note=Transported into peroxisomes CC following association with PEX7. {ECO:0000269|PubMed:22057399, CC ECO:0000269|PubMed:25538232}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P09110-1; Sequence=Displayed; CC Name=2; CC IsoId=P09110-2; Sequence=VSP_046195, VSP_046196; CC -!- INDUCTION: Peroxisomal thiolase is markedly induced (at the level of CC transcription) by various hypolipidemic compounds in parallel with the CC other two enzymes of the peroxisomal beta-oxidation system. CC {ECO:0000250|UniProtKB:P21775}. CC -!- DOMAIN: The PTS2-type peroxisomal targeting signal, which mediates CC interaction with PEX7 and localization to peroxisomes, is cleaved CC following import into peroxisomes. {ECO:0000305|PubMed:22057399, CC ECO:0000305|PubMed:25538232}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000305}. CC -!- CAUTION: Peroxisomal beta-oxidation of VLCFAs is likely partial, CC enabling formation of chain-shortened fatty acids that are further CC esterified in endoplasmic reticulum to form membrane lipids or routed CC to mitochondria for full oxidation and ATP production. The experimental CC data are scarce and some reactions in this entry are inferred from CC combined genetic interaction or mutant phenotype evidence and direct CC experimental evidence in parent reaction. {ECO:0000303|PubMed:10903473, CC ECO:0000303|PubMed:35951481}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X12966; CAA31412.1; -; mRNA. DR EMBL; X14813; CAA32918.1; -; mRNA. DR EMBL; X65140; CAA46270.1; -; Genomic_DNA. DR EMBL; X65148; CAA46271.1; -; Genomic_DNA. DR EMBL; AP006309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64516.1; -; Genomic_DNA. DR EMBL; BC000635; AAH00635.1; -; mRNA. DR EMBL; BC011977; AAH11977.1; -; mRNA. DR EMBL; BC014474; AAH14474.1; -; mRNA. DR CCDS; CCDS2673.1; -. [P09110-1] DR CCDS; CCDS46794.1; -. [P09110-2] DR PIR; S17515; XUHUAB. DR RefSeq; NP_001123882.1; NM_001130410.2. [P09110-2] DR RefSeq; NP_001598.1; NM_001607.4. [P09110-1] DR PDB; 2IIK; X-ray; 2.55 A; A/B=30-424. DR PDB; 9OK4; X-ray; 2.28 A; A/B=30-424. DR AlphaFoldDB; P09110; -. DR SMR; P09110; -. DR BioGRID; 106548; 98. DR FunCoup; P09110; 958. DR IntAct; P09110; 38. DR MINT; P09110; -. DR NDEx; IQUERY-CP-ACAA1; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000333664; -. DR CarbonylDB; P09110; -. DR GlyGen; P09110; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; P09110; -. DR MetOSite; P09110; -. DR PhosphoSitePlus; P09110; -. DR SwissPalm; P09110; -. DR BioMuta; ACAA1; -. DR DMDM; 135751; -. DR REPRODUCTION-2DPAGE; IPI00012828; -. DR jPOST; P09110; -. DR MassIVE; P09110; -. DR PaxDb; 9606-ENSP00000333664; -. DR PeptideAtlas; P09110; -. DR ProteomicsDB; 33816; -. DR ProteomicsDB; 52200; -. [P09110-1] DR Pumba; P09110; -. DR Antibodypedia; 1631; 333 antibodies from 35 providers. DR DNASU; 30; -. DR Ensembl; ENST00000301810.11; ENSP00000301810.7; ENSG00000060971.20. [P09110-2] DR Ensembl; ENST00000333167.13; ENSP00000333664.8; ENSG00000060971.20. [P09110-1] DR Ensembl; ENST00000896221.1; ENSP00000566280.1; ENSG00000060971.20. [P09110-1] DR GeneID; 30; -. DR KEGG; hsa:30; -. DR MANE-Select; ENST00000333167.13; ENSP00000333664.8; NM_001607.4; NP_001598.1. DR UCSC; uc003cht.4; human. [P09110-1] DR AGR; HGNC:82; -. DR ClinPGx; PA24419; -. DR CTD; 30; -. DR DisGeNET; 30; -. DR GeneCards; ACAA1; -. DR HGNC; HGNC:82; ACAA1. DR HPA; ENSG00000060971; Group enriched (kidney, liver). DR MalaCards; ACAA1; -. DR MIM; 604054; gene. DR OpenTargets; ENSG00000060971; -. DR VEuPathDB; HostDB:ENSG00000060971; -. DR eggNOG; KOG1389; Eukaryota. DR GeneTree; ENSGT01030000234626; -. DR InParanoid; P09110; -. DR OMA; QMGMDHL; -. DR OrthoDB; 5404651at2759; -. DR PAN-GO; P09110; 4 GO annotations based on evolutionary models. DR PhylomeDB; P09110; -. DR BioCyc; MetaCyc:HS00752-MONOMER; -. DR BRENDA; 2.3.1.16; 2681. DR PathwayCommons; P09110; -. DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism. DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins. DR SignaLink; P09110; -. DR UniPathway; UPA00661; -. DR Agora; ENSG00000060971; -. DR BioGRID-ORCS; 30; 22 hits in 1173 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ACAA1; human. DR EvolutionaryTrace; P09110; -. DR GeneWiki; ACAA1; -. DR GenomeRNAi; 30; -. DR Pharos; P09110; Tbio. DR PRO; PR:P09110; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P09110; protein. DR Bgee; ENSG00000060971; Expressed in jejunal mucosa and 206 other cell types or tissues. DR ExpressionAtlas; P09110; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:0008775; F:acetate CoA-transferase activity; EXP:Reactome. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB. DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISS:UniProtKB. DR GO; GO:0120524; F:long-chain fatty acyl-CoA oxidase activity; IMP:UniProtKB. DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome. DR GO; GO:0008206; P:bile acid metabolic process; IMP:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome. DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB. DR CDD; cd00751; thiolase; 1. DR FunFam; 3.40.47.10:FF:000035; 3-ketoacyl-CoA thiolase A, peroxisomal; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR050215; FADA-like. 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1. DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1. DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. DR PDBsum; 2IIK; -. DR PDBsum; 9OK4; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Alternative splicing; Fatty acid metabolism; KW Lipid metabolism; Peroxisome; Phosphoprotein; Proteomics identification; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..26 FT /note="Peroxisome" FT /evidence="ECO:0007744|PubMed:25944712" FT CHAIN 27..424 FT /note="3-ketoacyl-CoA thiolase, peroxisomal" FT /id="PRO_0000034067" FT REGION 1..26 FT /note="PTS2-type peroxisomal targeting signal" FT /evidence="ECO:0000269|PubMed:22057399, FT ECO:0000269|PubMed:25538232" FT ACT_SITE 123 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 377 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" FT ACT_SITE 408 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" FT MOD_RES 59 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 60 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 149..181 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046195" FT VAR_SEQ 272..331 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046196" FT VARIANT 172 FT /note="E -> D (in dbSNP:rs156265)" FT /id="VAR_011904" FT VARIANT 387 FT /note="V -> A (in dbSNP:rs2229528)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_069148" FT MUTAGEN 5 FT /note="Q->D,K,L: Does not affect localization to FT peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT MUTAGEN 6 FT /note="V->D: Abolished localization to peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT MUTAGEN 6 FT /note="V->K: Does not affect localization to peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT MUTAGEN 7 FT /note="V->D,K: Abolished localization to peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT MUTAGEN 8 FT /note="L->D,K: Does not affect localization to FT peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT MUTAGEN 9 FT /note="G->D,R,L: Does not affect localization to FT peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT MUTAGEN 10 FT /note="H->E: In S3E mutant; Abolished localization to FT peroxisomes." FT /evidence="ECO:0000269|PubMed:22057399" FT STRAND 38..45 FT /evidence="ECO:0007829|PDB:2IIK" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:2IIK" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 61..76 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 125..138 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 143..152 FT /evidence="ECO:0007829|PDB:2IIK" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 181..191 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 196..216 FT /evidence="ECO:0007829|PDB:2IIK" FT TURN 217..222 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 226..231 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 254..259 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 279..289 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 290..296 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 302..311 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 314..319 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 320..332 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 349..359 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 372..375 FT /evidence="ECO:0007829|PDB:2IIK" FT HELIX 379..397 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 401..409 FT /evidence="ECO:0007829|PDB:2IIK" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:2IIK" FT STRAND 413..421 FT /evidence="ECO:0007829|PDB:2IIK" SQ SEQUENCE 424 AA; 44292 MW; 71B2BBAFA06AE412 CRC64; MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLSDI PETVPLSTVN RQCSSGLQAV ASIAGGIRNG SYDIGMACGV ESMSLADRGN PGNITSRLME KEKARDCLIP MGITSENVAE RFGISREKQD TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI TVTQDEGIRP STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS QAAYCVEKLR LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR AYGVVSMCIG TGMGAAAVFE YPGN //