THIKB_MOUSE
ID THIKB_MOUSE Reviewed; 424 AA.
AC Q8VCH0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=3-ketoacyl-CoA thiolase B, peroxisomal {ECO:0000305};
DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P07871};
DE EC=2.3.1.16 {ECO:0000305|PubMed:15043762};
DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P07871};
DE AltName: Full=Acetyl-CoA acyltransferase B;
DE AltName: Full=Beta-ketothiolase B;
DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase B;
DE Flags: Precursor;
GN Name=Acaa1b {ECO:0000312|MGI:MGI:3605455}; Synonyms=Acaa1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP FUNCTION, AND PATHWAY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=15043762; DOI=10.1186/1471-2091-5-3;
RA Chevillard G., Clemencet M.-C., Etienne P., Martin P., Pineau T.,
RA Latruffe N., Nicolas-Frances V.;
RT "Molecular cloning, gene structure and expression profile of two mouse
RT peroxisomal 3-ketoacyl-CoA thiolase genes.";
RL BMC Biochem. 5:3-3(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Responsible for the thiolytic cleavage of straight chain 3-
CC keto fatty acyl-CoAs (3-oxoacyl-CoAs) (Probable). Plays an important
CC role in fatty acid peroxisomal beta-oxidation (Probable). Catalyzes the
CC cleavage of short, medium, long, and very long straight chain 3-
CC oxoacyl-CoAs (By similarity). {ECO:0000250|UniProtKB:P21775,
CC ECO:0000305|PubMed:15043762}.
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:0000305|PubMed:15043762};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000305|PubMed:15043762};
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:P07871};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC Evidence={ECO:0000250|UniProtKB:P07871};
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:0000305|PubMed:15043762};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000305|PubMed:15043762};
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:P07871};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000250|UniProtKB:P07871};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA +
CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084;
CC Evidence={ECO:0000250|UniProtKB:P07871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000250|UniProtKB:P07871};
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:0000250|UniProtKB:P09110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39132;
CC Evidence={ECO:0000250|UniProtKB:P09110};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:15043762}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P07871}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in liver; weaker levels in kidney,
CC intestine and white adipose tissue. {ECO:0000269|PubMed:15043762}.
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; AY273812; AAP31669.1; -; mRNA.
DR EMBL; BC019882; AAH19882.1; -; mRNA.
DR CCDS; CCDS23608.1; -.
DR RefSeq; NP_666342.1; NM_146230.3.
DR AlphaFoldDB; Q8VCH0; -.
DR SMR; Q8VCH0; -.
DR STRING; 10090.ENSMUSP00000010795; -.
DR CarbonylDB; Q8VCH0; -.
DR iPTMnet; Q8VCH0; -.
DR PhosphoSitePlus; Q8VCH0; -.
DR SwissPalm; Q8VCH0; -.
DR jPOST; Q8VCH0; -.
DR MaxQB; Q8VCH0; -.
DR PaxDb; Q8VCH0; -.
DR PeptideAtlas; Q8VCH0; -.
DR PRIDE; Q8VCH0; -.
DR ProteomicsDB; 262811; -.
DR Ensembl; ENSMUST00000010795; ENSMUSP00000010795; ENSMUSG00000010651.
DR GeneID; 235674; -.
DR KEGG; mmu:235674; -.
DR UCSC; uc009saj.1; mouse.
DR CTD; 235674; -.
DR MGI; MGI:3605455; Acaa1b.
DR VEuPathDB; HostDB:ENSMUSG00000010651; -.
DR eggNOG; KOG1389; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; Q8VCH0; -.
DR OMA; EPMRPGT; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; Q8VCH0; -.
DR TreeFam; TF332308; -.
DR BRENDA; 2.3.1.16; 3474.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 235674; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Acaa1b; mouse.
DR PRO; PR:Q8VCH0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VCH0; protein.
DR Bgee; ENSMUSG00000010651; Expressed in left lobe of liver and 185 other tissues.
DR ExpressionAtlas; Q8VCH0; baseline and differential.
DR Genevisible; Q8VCH0; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0008775; F:acetate CoA-transferase activity; ISO:MGI.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISO:MGI.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISO:MGI.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:MGI.
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 Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Peroxisome; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Peroxisome"
FT /evidence="ECO:0000250"
FT CHAIN 27..424
FT /note="3-ketoacyl-CoA thiolase B, peroxisomal"
FT /id="PRO_0000034069"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT ACT_SITE 408
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT BINDING 249
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT BINDING 252
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT BINDING 276
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT SITE 377
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921H8"
SQ SEQUENCE 424 AA; 43995 MW; 29BFFFF02DD43BAC CRC64;
MHRLQVVLGH LAGRPESSSA LQAAPCSAGF LQASASDVVV VHGRRTPIGR ASRGCFKDTT
PDELLSAVLT AVLQDVKLKP EQLGDISVGN VLQPGAGAIM ARIAQFLSGI PETVPLSTVN
RQCSSGLQAV ANIAGGIRNG SYDIGMACGV ESMTLSQRGN HGNISSRLLE NEKARDCLIP
MGITSENVAE RFGVSRQKQD AFALASQQKA ASAQSRGCFH AEIVPVTTTV LNDKGDKKTI
TVSQDEGVRP STTMQGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI
LGVLRSYAVV GVPPDVMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS QAVYCVEKLG
IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR AYGVVSMCIG TGMGAAAVFE
YPGN
