THILH_CAEEL
ID THILH_CAEEL Reviewed; 407 AA.
AC Q22100;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Acetyl-CoA acetyltransferase homolog, mitochondrial {ECO:0000305};
DE AltName: Full=3-ketoacyl-CoA thiolase {ECO:0000303|PubMed:20956318};
DE EC=2.3.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=kat-1 {ECO:0000312|WormBase:T02G5.8};
GN ORFNames=T02G5.8 {ECO:0000312|WormBase:T02G5.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CCD69179.1};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ALA-119.
RX PubMed=16462744; DOI=10.1038/ng1739;
RA Mak H.Y., Nelson L.S., Basson M., Johnson C.D., Ruvkun G.;
RT "Polygenic control of Caenorhabditis elegans fat storage.";
RL Nat. Genet. 38:363-368(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20956318; DOI=10.1073/pnas.1013854107;
RA Berdichevsky A., Nedelcu S., Boulias K., Bishop N.A., Guarente L.,
RA Horvitz H.R.;
RT "3-Ketoacyl thiolase delays aging of Caenorhabditis elegans and is required
RT for lifespan extension mediated by sir-2.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18927-18932(2010).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=24204312; DOI=10.1371/journal.pgen.1003908;
RA Soukas A.A., Carr C.E., Ruvkun G.;
RT "Genetic regulation of Caenorhabditis elegans lysosome related organelle
RT function.";
RL PLoS Genet. 9:E1003908-E1003908(2013).
CC -!- FUNCTION: Plays a role in ketone body metabolism (By similarity). Has
CC an effect on lysosome related organelles (LRO) function, in a pathway
CC with serotonin (PubMed:24204312). Acts downstream of sir-2.1 to
CC regulate aging and stress resistance (PubMed:20956318).
CC {ECO:0000250|UniProtKB:P24752, ECO:0000269|PubMed:20956318,
CC ECO:0000269|PubMed:24204312}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16462744}.
CC -!- DEVELOPMENTAL STAGE: Expressed in intestine from late embryogenesis
CC onwards, and in the body wall muscle and pharynx from L2 onwards.
CC {ECO:0000269|PubMed:16462744}.
CC -!- DISRUPTION PHENOTYPE: Animals have a shortened lifespan and exhibit
CC early behavioral decline characterized by the premature onset of
CC uncoordinated locomotion and paralysis. {ECO:0000269|PubMed:20956318}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; FO081112; CCD69179.1; -; Genomic_DNA.
DR PIR; T16781; T16781.
DR RefSeq; NP_495455.2; NM_063054.6.
DR AlphaFoldDB; Q22100; -.
DR SMR; Q22100; -.
DR DIP; DIP-25993N; -.
DR STRING; 6239.T02G5.8.2; -.
DR EPD; Q22100; -.
DR PaxDb; Q22100; -.
DR PeptideAtlas; Q22100; -.
DR EnsemblMetazoa; T02G5.8.1; T02G5.8.1; WBGene00002183.
DR GeneID; 174161; -.
DR KEGG; cel:CELE_T02G5.8; -.
DR UCSC; T02G5.8.1; c. elegans.
DR CTD; 174161; -.
DR WormBase; T02G5.8; CE29990; WBGene00002183; kat-1.
DR eggNOG; KOG1390; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_0_1_1; -.
DR InParanoid; Q22100; -.
DR OMA; TNVCCTT; -.
DR OrthoDB; 1011220at2759; -.
DR PhylomeDB; Q22100; -.
DR BRENDA; 2.3.1.16; 1045.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR Reactome; R-CEL-77108; Utilization of Ketone Bodies.
DR Reactome; R-CEL-77111; Synthesis of Ketone Bodies.
DR PRO; PR:Q22100; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002183; Expressed in germ line (C elegans) and 8 other tissues.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE 1: Evidence at protein level;
KW Acyltransferase; Metal-binding; Mitochondrion; Potassium;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..407
FT /note="Acetyl-CoA acetyltransferase homolog, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431836"
FT ACT_SITE 108
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000429-1"
FT ACT_SITE 365
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000429-1"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000429-1"
FT BINDING 201
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 201
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 244
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 260
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 261
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 263
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 264
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 361
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT MUTAGEN 119
FT /note="A->P: In mg368; increased uptake of the lipophilic
FT dye Nile Red and the synthetic fatty acid analog C1-BODIPY-
FT C12."
FT /evidence="ECO:0000269|PubMed:16462744,
FT ECO:0000269|PubMed:24204312"
SQ SEQUENCE 407 AA; 42443 MW; 65BA4F84282B1A19 CRC64;
MLSSSGHAIR RGITTSAALS NKHAFIVGAA RTPIGSFRSS LSSVTAPELA SVAIKAALER
GAVKPSSIQE VFLGQVCQAN AGQAPARQAA LGAGLDLSVA VTTVNKVCSS GLKAIILAAQ
QIQTGHQDFA IGGGMESMSQ VPFYVQRGEI PYGGFQVIDG IVKDGLTDAY DKVHMGNCGE
KTSKEMGITR KDQDEYAINS YKKSAKAWEN GNIGPEVVPV NVKSKKGVTI VDKDEEFTKV
NFDKFTSLRT VFQKDGTITA ANASTLNDGA AAVIVASQEA VSEQSLKPLA RILAYGDAAT
HPLDFAVAPT LMFPKILERA GVKQSDVAQW EVNEAFSCVP LAFIKKLGVD PSLVNPHGGA
VSIGHPIGMS GARLITHLVH TLKSGQIGVA AICNGGGGSS GMVIQKL
