ID   A0A0B7NJP3_9FUNG        Unreviewed;       398 AA.
AC   A0A0B7NJP3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Thiolase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=PARPA_09802.1 scaffold 39042 {ECO:0000313|EMBL:CEP15567.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP15567.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP15567.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP15567.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; LN732581; CEP15567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7NJP3; -.
DR   STRING; 35722.A0A0B7NJP3; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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   Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          6..268
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          275..397
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   398 AA;  41987 MW;  105BF1DBE9E5F86E CRC64;
     MPLRQVFIVS AKRTPFGAFG GKFKNLTGKS TRKFTAAAKA AIADLPQNVP IDSVIFGNVL
     QTDVAGAYVA RHIGHRAGLP VTVPALTVNR LCGSGLQSVV NAAQEIVLGE SEIVLAGGTE
     NMSLAPFTLS GSSRWGLKLG QDPKLQDTLW TALTDQYPTP TPMGITAENL AEKYNITKQE
     CDEYALSSQN RYEKAAKAGI YKNEIAPVEI KGRKGPELVS EDEHPRAGLQ MENLTKLKPV
     FKKDGVVSAA NASGINDGAA ALIVASEDAV KKYGLTPLAR IVSWQASAVE PTLMGLGPVP
     SIQGALKRAN LELKQMGLIE VNEAFAAQYL ACEKELGLER EITNVNGGAI AVGHPLGASG
     ARILTHLSHA LQRTKEKYAA GSACIGGGQG VAVILERA
//