ID A0A317XJ86_9BASI Unreviewed; 409 AA.
AC A0A317XJ86;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putative acetoacetyl-CoA thiolase {ECO:0000313|EMBL:PWY98376.1};
GN ORFNames=BCV70DRAFT_202153 {ECO:0000313|EMBL:PWY98376.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY98376.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWY98376.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY98376.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819199; PWY98376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XJ86; -.
DR STRING; 1882483.A0A317XJ86; -.
DR InParanoid; A0A317XJ86; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000246740};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 25..279
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 287..407
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 109
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 409 AA; 42359 MW; 5E4AA22D2D2EE445 CRC64;
MPAFYPTAVA RLSQTARIMS QIKDVYIISA ARTPVGSFNG SLKKATAPEL GTVAVKAAIE
RAGLKPDQIE EVYMGNVLQG NVGQAPARQV VLKSGCPEST EATTINKVCA SGMKSISLAA
QNIALGQRGI MVAGGMESMS NAPYYLPRGA ASFGHLQALD AIVKDGLHDV TNQVAMGVCA
ENTAKKLSLT REMQDAYAIE SYRRAADAWK AGAFANEIAP VTISDKKGDI VISEDEEYKN
VKLEKIPTLR PVFDKNGTVT AANASTLNDG ASAVVLASAD EVQKKGLKPL AKIVAFADAA
CAPIDFPIAP AYAIPKALEK AGLTTDDISL FEINEAFSAV ALANNQMLGL DASKVNVLGG
GVSLGHPIGS SGARIVVTLA HALKPGQYGC AGVCNGGGGA SAIIIKREA
//
