ID ECHB_RAT Reviewed; 475 AA. AC Q60587; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 165. DE RecName: Full=Trifunctional enzyme subunit beta, mitochondrial; DE AltName: Full=TP-beta; DE Includes: DE RecName: Full=3-ketoacyl-CoA thiolase; DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P55084}; DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P55084}; DE AltName: Full=Acetyl-CoA acyltransferase; DE AltName: Full=Beta-ketothiolase; DE Flags: Precursor; GN Name=Hadhb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; RX PubMed=8253773; DOI=10.1016/s0021-9258(19)74336-1; RA Kamijo T., Aoyama T., Miyazaki J., Hashimoto T.; RT "Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty RT acid beta-oxidation multienzyme complex. Structural and functional RT relationships to other mitochondrial and peroxisomal beta-oxidation RT enzymes."; RL J. Biol. Chem. 268:26452-26460(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; 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 [3] RP SUBUNIT. RX PubMed=1730633; DOI=10.1016/s0021-9258(18)48391-3; RA Uchida Y., Izai K., Orii T., Hashimoto T.; RT "Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. RT Purification and properties of enoyl-coenzyme A (CoA) hydratase/3- RT hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional RT protein."; RL J. Biol. Chem. 267:1034-1041(1992). CC -!- FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three CC of the four reactions of the mitochondrial beta-oxidation pathway. The CC mitochondrial beta-oxidation pathway is the major energy-producing CC process in tissues and is performed through four consecutive reactions CC breaking down fatty acids into acetyl-CoA. Among the enzymes involved CC in this pathway, the trifunctional enzyme exhibits specificity for CC long-chain fatty acids. Mitochondrial trifunctional enzyme is a CC heterotetrameric complex composed of two proteins, the trifunctional CC enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the CC 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional CC enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA CC thiolase activity. {ECO:0000250|UniProtKB:P55084}. 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 Evidence={ECO:0000250|UniProtKB:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + hexanoyl-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:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + octanoyl-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:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + decanoyl-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:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + dodecanoyl-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:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + tetradecanoyl-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:0000250|UniProtKB:P55084}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; CC Evidence={ECO:0000250|UniProtKB:P55084}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000250|UniProtKB:P55084}. CC -!- SUBUNIT: Heterotetramer of 2 alpha/HADHA and 2 beta/HADHB subunits; CC forms the mitochondrial trifunctional enzyme (By similarity). Also CC purified as higher order heterooligomers including a 4 alpha/HADHA and CC 4 beta/HADHB heterooligomer which physiological significance remains CC unclear (PubMed:1730633). The mitochondrial trifunctional enzyme CC interacts with MTLN (By similarity). Interacts with RSAD2/viperin (By CC similarity). {ECO:0000250|UniProtKB:P55084, CC ECO:0000250|UniProtKB:Q99JY0, ECO:0000269|PubMed:1730633}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P55084}. CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P55084}. CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55084}. CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P55084}. Note=Protein CC stability and association with membranes require HADHA. CC {ECO:0000250|UniProtKB:P55084}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000305}. 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; D16479; BAA03940.1; -; mRNA. DR EMBL; BC060545; AAH60545.1; -; mRNA. DR PIR; B49681; B49681. DR RefSeq; NP_598302.1; NM_133618.3. DR RefSeq; XP_006239848.2; XM_006239786.2. DR RefSeq; XP_006239850.1; XM_006239788.1. DR RefSeq; XP_006239851.1; XM_006239789.3. DR AlphaFoldDB; Q60587; -. DR SMR; Q60587; -. DR BioGRID; 251158; 5. DR IntAct; Q60587; 4. DR MINT; Q60587; -. DR STRING; 10116.ENSRNOP00000072480; -. DR CarbonylDB; Q60587; -. DR GlyGen; Q60587; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; Q60587; -. DR PhosphoSitePlus; Q60587; -. DR SwissPalm; Q60587; -. DR jPOST; Q60587; -. DR PaxDb; 10116-ENSRNOP00000014637; -. DR Ensembl; ENSRNOT00000014637.7; ENSRNOP00000014637.5; ENSRNOG00000010800.7. DR Ensembl; ENSRNOT00055034375; ENSRNOP00055027847; ENSRNOG00055020119. DR Ensembl; ENSRNOT00060020145; ENSRNOP00060015818; ENSRNOG00060011900. DR Ensembl; ENSRNOT00065041223; ENSRNOP00065033671; ENSRNOG00065024007. DR GeneID; 171155; -. DR KEGG; rno:171155; -. DR AGR; RGD:620513; -. DR CTD; 3032; -. DR RGD; 620513; Hadhb. DR eggNOG; KOG1392; Eukaryota. DR GeneTree; ENSGT01030000234626; -. DR InParanoid; Q60587; -. DR OrthoDB; 1826604at2759; -. DR PhylomeDB; Q60587; -. DR TreeFam; TF315243; -. DR Reactome; R-RNO-1482798; Acyl chain remodeling of CL. DR Reactome; R-RNO-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA. DR Reactome; R-RNO-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA. DR Reactome; R-RNO-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA. DR Reactome; R-RNO-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA. DR Reactome; R-RNO-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA. DR Reactome; R-RNO-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA. DR UniPathway; UPA00659; -. DR PRO; PR:Q60587; -. DR Proteomes; UP000002494; Chromosome 6. DR Bgee; ENSRNOG00000010800; Expressed in heart and 20 other cell types or tissues. DR ExpressionAtlas; Q60587; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IDA:RGD. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD. DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISO:RGD. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:RGD. DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0106222; F:lncRNA binding; ISO:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD. DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1. DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1. DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 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 Genevisible; Q60587; RN. PE 1: Evidence at protein level; KW Acetylation; Acyltransferase; Endoplasmic reticulum; Fatty acid metabolism; KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Mitochondrion outer membrane; Reference proteome; Transferase; KW Transit peptide. FT TRANSIT 1..34 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 35..475 FT /note="Trifunctional enzyme subunit beta, mitochondrial" FT /id="PRO_0000034084" FT INTRAMEM 174..221 FT /evidence="ECO:0000250|UniProtKB:P55084" FT ACT_SITE 139 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250|UniProtKB:P55084" FT ACT_SITE 459 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P55084" FT SITE 429 FT /note="Increases nucleophilicity of active site Cys" FT /evidence="ECO:0000250|UniProtKB:P55084" FT MOD_RES 53 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 73 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P55084" FT MOD_RES 73 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 189 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P55084" FT MOD_RES 189 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 191 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 273 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 292 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 294 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 294 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 299 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 333 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 333 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 349 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" FT MOD_RES 362 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99JY0" SQ SEQUENCE 475 AA; 51414 MW; 59231029C8BA2A13 CRC64; MTTILTSTFR NLSTTSKWAL RFSVRPLSCS SQVQSAPAVQ TKSKKTLAKP NLKNIVVVEG VRIPFLLSGT SYKDLMPHDL ARAALSGLLY RTNIPKDVVD YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV GLIASGQCDV VVAGGVELMS DVPIRHSRNM RKMMLDLNKA KTLAQRLSLL TKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM EQDKYALRSH SLAKKAQDEG HLSDIVPFKV PGKDTVSKDN GIRPSSLEQM AKLKPAFIKP YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD QLLLGPTYAT PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA QNYMGRKTKV GAPPLEKFNI WGGSLSLGHP FGATGCRLVM AAANRLRKDG GQYALVAACA AGGQGHAMIV EAYPK //