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Database: UniProt
Entry: A0A0N4ZAU2_PARTI
LinkDB: A0A0N4ZAU2_PARTI
Original site: A0A0N4ZAU2_PARTI 
ID   A0A0N4ZAU2_PARTI        Unreviewed;       396 AA.
AC   A0A0N4ZAU2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=3-ketoacyl-CoA thiolase, mitochondrial {ECO:0008006|Google:ProtNLM};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000465600.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000465600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR   AlphaFoldDB; A0A0N4ZAU2; -.
DR   STRING; 131310.A0A0N4ZAU2; -.
DR   WBParaSite; PTRK_0000465600.1; PTRK_0000465600.1; PTRK_0000465600.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
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; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          8..265
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          274..395
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        93
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        352
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   396 AA;  41869 MW;  9C32A2E7EDF46148 CRC64;
     MTGLSKGIFI VGAKRTPFGT FGGTLKNHSA TDLQVIANKA AIQSAAIKPE EIDHVIIGNV
     AQTSKDAIYL ARHSALKVGI PVPVPAVTVN RLCGSGFQSV VDGCLQILAG DSNVVLAGGT
     ESMSQAPFIV RGTRFGTTFG KPIEFEDSLW SGLTDQYIKT PMALTAEKLG DMYKISRRDV
     DEYALNSQLR WSLANNDGVF KREITPITIK GKKGDVKFEV DEHPRLTTIE KLSGLPPVFK
     KDGIVTAGNA SGICDGAAAC ILASDSAVER LKLEPLVRIV GWHATGCDPS IMGIGPVPAI
     QALVKKTGVS LDKVGLIEIN EAFGAQVLAC QKELKIDMDK FNINGGAIAL GHPLGASGNR
     ILVHLAHNMK HKNVQYGIGS ACIGGGQGIA VLLERI
//
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