ID   W6YVD6_COCMI            Unreviewed;       434 AA.
AC   W6YVD6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Acetyl-CoA acetyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=COCMIDRAFT_105956 {ECO:0000313|EMBL:EUC41510.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC41510.1};
RN   [1] {ECO:0000313|EMBL:EUC41510.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC41510.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR   EMBL; KI964099; EUC41510.1; -; Genomic_DNA.
DR   RefSeq; XP_007691973.1; XM_007693783.1.
DR   AlphaFoldDB; W6YVD6; -.
DR   STRING; 930090.W6YVD6; -.
DR   GeneID; 19118776; -.
DR   KEGG; bor:COCMIDRAFT_105956; -.
DR   eggNOG; KOG1390; Eukaryota.
DR   HOGENOM; CLU_031026_0_0_1; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000054032; 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; 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.
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   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          41..298
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          309..428
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        124
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        387
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        415
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   434 AA;  45727 MW;  5413A3ACC1B9BFC3 CRC64;
     MSSAVIRNSF KMASRPQQRL ASIQRQFSSS APQRKEIRDA YILSASRTPT AVFNGNFTTV
     SAPQLGATAI KSALEKSKVP VSSIDAVYMG NVLGGGVGQA PARQAAIFAG LPTNIEATTI
     NKVCASGLKA VSIAASTIEL GQAEAQVAGG MENMTRVPYY LSRASQQPAF GHQKLEDGLI
     SDGLWDVYNQ IHMGNCAENT AKKYEVSRQD QDDYAIETYK RAQQAYKDGL FKDEIVPVTV
     KTRKGETVVS EDEQYNKLKL DKVATLKPAF EKGPNGSVTA ANSSPLSDGA SALVLGSKDI
     AQKYGKDSRV LAKIVTYADA ALDPIDFPVA PAACVDKLLA QSGLSKSDIA IWEFNEAFAA
     VIKANAKILG LGTENVNPRG GAIALGHALG SSGSRILVTL LHQLKDGQYG AAVICNGGGA
     ASGIIVQKVS ADQL
//