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Database: UniProt
Entry: A0A0V1PG79_9BILA
LinkDB: A0A0V1PG79_9BILA
Original site: A0A0V1PG79_9BILA 
ID   A0A0V1PG79_9BILA        Unreviewed;       417 AA.
AC   A0A0V1PG79;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Acetyl-CoA acetyltransferase, mitochondrial {ECO:0000313|EMBL:KRZ95236.1};
GN   Name=acat1 {ECO:0000313|EMBL:KRZ95236.1};
GN   ORFNames=T08_6943 {ECO:0000313|EMBL:KRZ95236.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ95236.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ95236.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ95236.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ95236.1}.
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DR   EMBL; JYDM01000013; KRZ95236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1PG79; -.
DR   STRING; 92180.A0A0V1PG79; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
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; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
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:SF156; ACETYL-COA ACETYLTRANSFERASE, 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; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          31..287
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          297..416
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        115
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        375
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   417 AA;  44598 MW;  BAABAB239F71D9FB CRC64;
     MNLLKVVSFF NSKVELVSSS KRFMSGDLQK VYILSACRTP IGSFRSAFAS MKAPELGSIA
     IKAAVDQADI PPQIIEEVYM GNVLQAYSGQ APARQALIGA GLPNSIPATT VNNVCASGLK
     AAMIAAQNLM CNHSETIVAG GMESMSNVPF YLPRTEIPYG GTAIKDGIVY DGLWDVYNQI
     HMGSCAEKTA KEQCISREAQ DEYAKLSYER SASAWKRGVF NDEVVPVTVK QRDNVKIVSE
     DEEYKKCDFS RFASLKPVFN KDGGTGTITA ANASTLNDGA CALVLMNAVG IEKYSAKPKA
     EIICFAEIAT APIDFPIAPA AAIEKVLKIS GMKKEDIALW EINEAFSVVA LANMKLLQLE
     KSKVNIHGGA VSIGHPLGMS GARILTHLVH SLKPNEYGIA AICYGGGGAS AMLIKKI
//
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