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
//