ID A0A1X6NG46_9APHY Unreviewed; 411 AA.
AC A0A1X6NG46;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=POSPLADRAFT_1042816 {ECO:0000313|EMBL:OSX67609.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX67609.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX67609.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX67609.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) 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; KZ110591; OSX67609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6NG46; -.
DR STRING; 670580.A0A1X6NG46; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000194127; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF10; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 34..277
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 287..405
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 364
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 411 AA; 43376 MW; D1929BF88F833476 CRC64;
MFPRLVRSAV PRVRSLSTQV GGVAAILERK PDDVVITFAK RTALGRAKKG QLKDVPVDEL
MQALIKATLE KTKLDPAKLE DICVGTCHSP SPTYVSRAAA IAAGVPVEVP VSAVNRLCGS
GLQAIRIIAN AIQAGHMSLG MAIGVENMSL NPRPTPEIVE GVEAIPQAHD CVQPMGWTSE
MVAEAYKISR QKQDEYALIS HTRAEKASEA GIFGEEIMPV ELRGTIISVD DTIRKGTTAE
GLSKLKPAFP AWGEASSTGG NSSGLGDGAA LCILTTRKRA EKEGMEIIGK YVATSFVGVE
PRYMGIAPVA AIPKVLEQTG LAKEDVDVYE INEAFASQFA YCVEQLDVPM SKVNPNGGSI
ALSHPLGMTG VRQVVTGLAQ LRRQGGNILC TSMCIGSGMG GAGIFVNEAH A
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