ECHB_PANTR
ID ECHB_PANTR Reviewed; 475 AA.
AC Q5R1W7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N.,
RA Hashimoto K.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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. Also purified as higher
CC order heterooligomers including a 4 alpha/HADHA and 4 beta/HADHB
CC heterooligomer which physiological significance remains unclear. The
CC mitochondrial trifunctional enzyme interacts with MTLN. Interacts with
CC RSAD2/viperin. {ECO:0000250|UniProtKB:P55084,
CC ECO:0000250|UniProtKB:Q8BMS1}.
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}.
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DR EMBL; AB188280; BAD74031.1; -; mRNA.
DR RefSeq; NP_001029291.1; NM_001034119.1.
DR RefSeq; XP_009440359.1; XM_009442084.2.
DR AlphaFoldDB; Q5R1W7; -.
DR SMR; Q5R1W7; -.
DR STRING; 9598.ENSPTRP00000020160; -.
DR PaxDb; Q5R1W7; -.
DR Ensembl; ENSPTRT00000021854; ENSPTRP00000020160; ENSPTRG00000011733.
DR GeneID; 459080; -.
DR KEGG; ptr:459080; -.
DR CTD; 3032; -.
DR VGNC; VGNC:48985; HADHB.
DR eggNOG; KOG1392; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_2_0_1; -.
DR InParanoid; Q5R1W7; -.
DR OrthoDB; 1129049at2759; -.
DR TreeFam; TF315243; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002277; Chromosome 2A.
DR Bgee; ENSPTRG00000011733; Expressed in heart and 21 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006635; P:fatty acid beta-oxidation; 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 2: Evidence at transcript 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:0000255"
FT CHAIN 35..475
FT /note="Trifunctional enzyme subunit beta, mitochondrial"
FT /id="PRO_0000034083"
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 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; 51396 MW; 123CA01ABD00CBAE CRC64;
MTTILTYPFK NLPTASKWAL RFSIRPLSCS SQLRAAPAVQ TKTKKTLAKP NIRNVVVVDG
VRTPFLLSGT SYKDLMPHDL ARAALTGLLH RTSVPKEVVD YIIFGTVIQE VKTSNVAREA
ALGAGFSDKT PAHTVTMACI SANQAMTTGV GLIASGQCDV IVAGGVELMS DVPIRHSRKM
RKLMLDLNKA KSMGQRLSLI SKFRFNFLAP ELPAVSEFST SETMGHSADR LAAAFAVSRL
EQDEYALRSH SLAKKAQDEG LLSDVVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP
YGTVTAANSS FLTDGASAML IMAEEKALAM GYKPKAYLRD FMYVSQDPKD QLLLGPTYAT
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA ENYMGRKTKV GLPPLEKFNN
WGGSLSLGHP FGATGCRLVM AAANRLRKEG GQYGLVAACA AGGQGHAMIV EAYPK
