ID A0A316VJ48_9BASI Unreviewed; 420 AA.
AC A0A316VJ48;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=FA14DRAFT_168014 {ECO:0000313|EMBL:PWN36323.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN36323.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN36323.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN36323.1,
RC ECO:0000313|Proteomes:UP000245771};
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; KZ819603; PWN36323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VJ48; -.
DR STRING; 1280837.A0A316VJ48; -.
DR InParanoid; A0A316VJ48; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000245771; 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; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF5; 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; 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 ECO:0000313|EMBL:PWN36323.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245771};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PWN36323.1}.
FT DOMAIN 31..289
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 299..418
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 118
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 406
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 420 AA; 44742 MW; 94812FEB7BFC73A7 CRC64;
MSFARGAFRV SATLRDKSAL EGILKKRPDD VVFTTALRTP VARMKKGYKD AYPEELLAFV
LQRTRERLEN KGVSIDAIED ICTGTVLMEL GGAKSGRLAA LHAGMPITSA YSTVNRQCAS
SLQSITNIAQ SIQTGQIAVG IAAGVESMTR DWGTRAIPVK LSPAMAQSPN QDARDCLMSM
GLTSENVAAQ WKIGRDEQDE FAATSQQRAA AAQEDGRLAQ EIEPIEVRWM DDAGNETTRL
VEKDEGVRKG TTKETLAKLK PAFKEDGTST AGNSSQVSDG AVALTMARRD VAEKLGMEIL
GKWVGTSTIG VKPDIMGVGP AYASPKLLNR FGLDAKEIDL WEINEAFASQ VLMTMGHLGI
SHDQVNVKGG AIALGHPLGA SGGRLVTSLL SELRRTGKQT GVATLCCGTG YGKASLIVAE
//
