ECHH_CAEEL
ID ECHH_CAEEL Reviewed; 448 AA.
AC P34255;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable 3-ketoacyl-CoA thiolase {ECO:0000305};
DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P55084};
GN ORFNames=B0303.3 {ECO:0000312|WormBase:B0303.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1538779; DOI=10.1038/356037a0;
RA Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA Waterston R.;
RT "The C. elegans genome sequencing project: a beginning.";
RL Nature 356:37-41(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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).
CC -!- FUNCTION: Mitochondrial enzyme that catalyzes reactions of the
CC mitochondrial beta-oxidation pathway. {ECO:0000305}.
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 -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P55084}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {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; BX284603; CCD61708.1; -; Genomic_DNA.
DR PIR; S27785; S27785.
DR RefSeq; NP_498915.1; NM_066514.4.
DR AlphaFoldDB; P34255; -.
DR SMR; P34255; -.
DR BioGRID; 41419; 11.
DR IntAct; P34255; 1.
DR STRING; 6239.B0303.3.1; -.
DR EPD; P34255; -.
DR PaxDb; P34255; -.
DR PeptideAtlas; P34255; -.
DR EnsemblMetazoa; B0303.3.1; B0303.3.1; WBGene00015125.
DR EnsemblMetazoa; B0303.3.2; B0303.3.2; WBGene00015125.
DR GeneID; 176216; -.
DR KEGG; cel:CELE_B0303.3; -.
DR UCSC; B0303.3.2; c. elegans.
DR CTD; 176216; -.
DR WormBase; B0303.3; CE00561; WBGene00015125; -.
DR eggNOG; KOG1392; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_2_0_1; -.
DR InParanoid; P34255; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; P34255; -.
DR Reactome; R-CEL-1482798; Acyl chain remodeling of CL.
DR Reactome; R-CEL-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
DR Reactome; R-CEL-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
DR Reactome; R-CEL-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR Reactome; R-CEL-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-CEL-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR Reactome; R-CEL-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR UniPathway; UPA00659; -.
DR PRO; PR:P34255; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015125; Expressed in embryo and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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 PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
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 3: Inferred from homology;
KW Acyltransferase; Fatty acid metabolism; Lipid metabolism; Mitochondrion;
KW Reference proteome; Transferase.
FT CHAIN 1..448
FT /note="Probable 3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206464"
FT ACT_SITE 110
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P55084"
FT ACT_SITE 402
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ SEQUENCE 448 AA; 47874 MW; F607B9B4690F2EB3 CRC64;
MLRAVSTSFG TARAASAVAK KNMPNIVLVD AVRTPFVVSG TVFKDLMAVD LQKEAIKALV
EKTKLPYEQL DHIICGTVIQ ECKTSNIARE AALLAGVPDK IPAHTVTLAC ISSNVAMTTG
MGMLATGNAN AIIAGGVELL SDVPIRYNRN ARKAMLGMNK AKDVPSKLKI GGQIVKNLLS
PELPAVAEFS TGETMGHSGD RLAAAFNVSR REQDEFAIRS HTLASEAAKN GKFTDVVPVF
LDGKKPKTIK EDNGIRVSTL EKLSSLKPAF VKPHGTVTAA NASYLTDGAS AALIMTEEYA
LANGYKPKAY LRDYLYVAQD PKDQLLLSPA YVIPKLLDKA GLTLKDVDVF EIHEAFAGQV
LANLNAMDSD YFCKEQMKRS GKFGRVPMDK LNLWGGSLSI GHPFGATGVR LATHSAHRLK
EEKGQYAVIA ACAAGGHGVG MLIEAYGK
