ID   Q7SYR2_XENLA            Unreviewed;       419 AA.
AC   Q7SYR2;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=3-ketoacyl-CoA thiolase, peroxisomal {ECO:0000313|RefSeq:NP_001080604.1};
DE            EC=2.3.1.16 {ECO:0000313|RefSeq:NP_001080604.1};
DE   SubName: Full=Acaa1-prov protein {ECO:0000313|EMBL:AAH54299.1};
GN   Name=acaa1.L {ECO:0000313|RefSeq:NP_001080604.1,
GN   ECO:0000313|Xenbase:XB-GENE-963073};
GN   Synonyms=acaa1 {ECO:0000313|RefSeq:NP_001080604.1,
GN   ECO:0000313|Xenbase:XB-GENE-963073};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH54299.1};
RN   [1] {ECO:0000313|RefSeq:NP_001080604.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH54299.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAH54299.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001080604.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037000};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC         Evidence={ECO:0000256|ARBA:ARBA00037000};
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:0000256|ARBA:ARBA00036770};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39132;
CC         Evidence={ECO:0000256|ARBA:ARBA00036770};
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:0000256|ARBA:ARBA00024540};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC         Evidence={ECO:0000256|ARBA:ARBA00024540};
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:0000256|ARBA:ARBA00024485};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC         Evidence={ECO:0000256|ARBA:ARBA00024485};
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:0000256|ARBA:ARBA00024462};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC         Evidence={ECO:0000256|ARBA:ARBA00024462};
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:0000256|ARBA:ARBA00024455};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC         Evidence={ECO:0000256|ARBA:ARBA00024455};
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00004846}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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; BC054299; AAH54299.1; -; mRNA.
DR   RefSeq; NP_001080604.1; NM_001087135.1.
DR   DNASU; 380296; -.
DR   GeneID; 380296; -.
DR   KEGG; xla:380296; -.
DR   AGR; Xenbase:XB-GENE-963073; -.
DR   CTD; 380296; -.
DR   Xenbase; XB-GENE-963073; acaa1.L.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 380296; Expressed in liver and 19 other cell types or tissues.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 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.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000256|RuleBase:RU003557};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          33..285
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          294..415
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        118
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        403
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   419 AA;  43758 MW;  6441471524B1B9ED CRC64;
     MHRVRVVLGH LPANSRGVWA ENSSASADKS QDIVIVAGRR TPICKAKRGA FKETTPDELL
     STVMTAVLKD VNVSPELLGD ICVGNVLQPG AGALVARIGQ FLSGIPESVP IHVVNRQCSS
     GLQAIINVAG GIRNGSYDIG LACGMESMSL RSVGSPGDIS SRTMDFSKAR DCLIPMGITS
     ENVAEKFGVT REKQDSLALA SQQRAAAAQR SGRFKAEIVP VTTTFTDDQG NTKTITVTED
     EGVRASTTME GLSRLKPAFK EGGSTTAGNS SQVSDGAAAV LMAKRSRAEQ LGLPILGVLR
     SFAVVGVPPD VMGIGPAYAI PAALQKAGLT VHDIDVYEIN EAFASQAVYC VEKLGIPVEK
     VNPNGGAIAL GHPLGCTGTR QTVTLLNELK RRGKRGFGVV SMCIGTGMGA AAVYEYPGH
//