ID   C4JNH3_UNCRE            Unreviewed;       420 AA.
AC   C4JNH3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EEP78126.1};
GN   ORFNames=UREG_02971 {ECO:0000313|EMBL:EEP78126.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP78126.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476616; EEP78126.1; -; Genomic_DNA.
DR   RefSeq; XP_002543455.1; XM_002543409.1.
DR   AlphaFoldDB; C4JNH3; -.
DR   STRING; 336963.C4JNH3; -.
DR   GeneID; 8438990; -.
DR   KEGG; ure:UREG_02971; -.
DR   VEuPathDB; FungiDB:UREG_02971; -.
DR   eggNOG; KOG1390; Eukaryota.
DR   HOGENOM; CLU_031026_0_1_1; -.
DR   InParanoid; C4JNH3; -.
DR   OMA; SMGTFGE; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000002058; 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   Reference proteome {ECO:0000313|Proteomes:UP000002058};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EEP78126.1}.
FT   DOMAIN          29..286
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          297..416
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        112
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        403
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   420 AA;  44648 MW;  989DE10F84582EE0 CRC64;
     MPQASQRLAQ VQRQFSSSTA RRREIQDAYI LSAARTPTAK FNGSFVTVPA PQLGAVAIKA
     AVEKSKIPME KITDVYMGCV LQGSVGQAPA RQASMFAGLP SSVEALTVNK VCASGMKAVI
     LAAQNIQLGL AEAQVAGGME NMSRVPYYYP RASQQPAFGN ATMEDGLIKD GLWDVYNQFH
     MGVCAENTAK KYNITRQEQD EYAVRSYQRA QAAWKENKFA DEIAPVTVKS RKGEVVVSRD
     EGFEDLRADK MASLKPAFVR DGTGTVTAGN ASTFNDGASA LVITNEALAR EHSSGNRVLA
     RIVSSADAAI DPVDFPVAPA KAVPIALERA GLTKDQISIW EFNEAFAAVI KANEKILGLE
     NANVNPLGGA ISLGHALGSS GSRILTTLLH QLKPGEYGCA AICNGGGAAT AIIVQRVEKI
//