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Database: UniProt
Entry: A0A094AB93_9PEZI
LinkDB: A0A094AB93_9PEZI
Original site: A0A094AB93_9PEZI 
ID   A0A094AB93_9PEZI        Unreviewed;       419 AA.
AC   A0A094AB93;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE            EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN   ORFNames=V493_03966 {ECO:0000313|EMBL:KFY26659.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY26659.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY26659.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
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:KFY26659.1}.
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DR   EMBL; JPJV01001539; KFY26659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AB93; -.
DR   STRING; 1420906.A0A094AB93; -.
DR   HOGENOM; CLU_031026_1_1_1; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43853:SF12; ACETYL-COA C-ACETYLTRANSFERASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000029327};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          33..288
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          297..415
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        117
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        374
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        404
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   419 AA;  43961 MW;  119CB499A0C822FE CRC64;
     MSSAQSRLSS VMGHLGSPGD GKARLLQKNP DDIVITLAIR TPLTKARKGG LKDTPIDDLL
     IAILTQVREK SKLDPGLVED ICVGNCLASG QAYIARSAVL AAGFPVTTAA SVANRFCSSG
     LLAIQGIANQ ISAGSIDVGI AVGAESMSTT PDDGAPKMSE KITNHPIATQ NQMSMGYTSE
     EVAGQFDVSR QAMDQFAAES YQKAEKAQKE GWFADEITPI VVTIKDPKTG EAKQATISKD
     DGVRYGTTAE SLGKIRNAFP QWKPSRTTGG NASQITDGGA AVLLMKRSRA IELGQPIIGK
     FAGATVVGLE PRIMGIGPSY AIPKILGKVG LTKEDVDVFE INEAFASMGV YCVEKLALDK
     AKVNPRGGAI ALGHPLGCTG ARQVVTALSE LRRQNRRIAV TSMCVGTGMG MAGIFVSEH
//
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