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Database: UniProt
Entry: A0A1I8BJ64_MELHA
LinkDB: A0A1I8BJ64_MELHA
Original site: A0A1I8BJ64_MELHA 
ID   A0A1I8BJ64_MELHA        Unreviewed;       471 AA.
AC   A0A1I8BJ64;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE            EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig277.frz3.gene31};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig277.frz3.gene31}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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; A0A1I8BJ64; -.
DR   WBParaSite; MhA1_Contig277.frz3.gene31; MhA1_Contig277.frz3.gene31; MhA1_Contig277.frz3.gene31.
DR   OMA; MTAFPEP; -.
DR   Proteomes; UP000095281; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 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|RuleBase:RU003557}.
FT   DOMAIN          48..322
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          330..468
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   471 AA;  51265 MW;  E83473BF22D6F133 CRC64;
     MIFLAKHQNL LFNSSVNLFK NKSLKTVLVS NASITTQQQS TPNTRPNVVL IDAVRTPFVL
     SNTVFRELLA VDLQRHALRA LVDRTNVPFE DIGHIICGQV VQECKTSNIA REAAITAGFP
     DSIPCNTVTL ACISSAVSTQ NIASMISNGY LKAGIAGGVE LLSDFPVRYN RKARLSMIDF
     QKAKKLDAKL KYGFKMLANW FTPELPAVSE FTTGEVMGNS GDRLAAAFNV SRKEQDDFAI
     RSHTFAEKAT KENKLIDVVP MFVPYGPKKG QTVLTDNGIR VSTTEQMAKL KAAFIKPHGT
     VTAGNSSYLT DGASAALISS ESYALQKGYK PKAFIRETMF VAQDPKDQLL LSPAYVIPKL
     LDKVGLKLQD IDVFEIHEAF AGQLLANLKA LDSDWFCQNY MKRSGKFGVL PLEKLNLWGG
     SLSLGHPFGA TGVRLLAHAA NRLKDEGGRY AVIAACAAGG HGVGMLVEAY K
//
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