ID C0NJW7_AJECG Unreviewed; 417 AA.
AC C0NJW7;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=HCBG_03447 {ECO:0000313|EMBL:EEH08158.1}, HCBG_03496
GN {ECO:0000313|EMBL:EEH08207.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH08158.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEH08158.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G186AR {ECO:0000313|EMBL:EEH08158.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000617};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
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; GG663366; EEH08158.1; -; Genomic_DNA.
DR EMBL; GG663366; EEH08207.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NJW7; -.
DR STRING; 447093.C0NJW7; -.
DR VEuPathDB; FungiDB:I7I50_07099; -.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; C0NJW7; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 32..287
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 296..413
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 117
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 373
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 417 AA; 43453 MW; 987F681668CFEBA9 CRC64;
MSQATQRLSQ VTSHLTGKGG VSAITAKHPD DIVVTCALRT AITKGGKGGF KDTAASDLLA
GVFKSLVEKS KIDPALVEDI AVGSVLPPGG GATEFRAAAL VAGFPETAAV RSLNRQCSSG
LQAIVDIANA IKCGMIDVGI GAGVESMSQQ YGPGAVSEFS ELLESNQEAA NCKVPMGILS
EQMAKDRNIT RAEQDAFAAT SYQKAVKAQE AGLFNEEIAP QTVKFVDPKT EKESTITVSR
DDGVRTGITA ESLSKIRPAF AKDGSIHAGN SSQISDGAAA VLLMKRSTAE RLGQRIIGKY
VTASVVGVKP LLMGIGPWKA IPVALEKAGL SRDDVDIYEI NEAFASQCVW CVKELGLPLE
KVNPKGGAIA FGHPLGCTGC RQVSTLLTEL KRTGKRVGVT SMCVGTGMGM AAVWVAE
//
