ID A0A0C3BP03_HEBCY Unreviewed; 407 AA.
AC A0A0C3BP03;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=M413DRAFT_447863 {ECO:0000313|EMBL:KIM38400.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM38400.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM38400.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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 -!- 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; KN831791; KIM38400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3BP03; -.
DR STRING; 686832.A0A0C3BP03; -.
DR HOGENOM; CLU_031026_1_1_1; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000053424; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000053424};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 20..275
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 285..403
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 105
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 407 AA; 41911 MW; 1A9C0EBF8CC1067C CRC64;
MSTQTSPQKE SVLQKHDNDV VIVSAVRSAI TKGRKGGFKD TKPELILAHV LRAAYTKADV
DPTLIEDVAV GNCLLPGAGA GHARVAAIHA GIPIDASVNT VNRQCSSGLS AINQIANQIR
VGQIDIGIGA GVESMTFGGF GSGGKASYSE EAMATQDAKD CLIPMGITSE NVASDYGLSR
QVQDEFAAKS FQKAAAAAKA GKFRDEIVPM KVKSVDAKTG EITEIVVAED DGIRDGVTVE
SLSKLKPAFT KDGSTHAGNA SQVSDGAAAV LLARRSVALR LGLPIIGKFV AAATVGVPPR
IMGVGPAYAI PRVLALTSLS LSDVDFYEIN EAFASQAIFS VQHLGIPFEK VNVNGGAIAM
GHPLGCTGAR QVATGLSVAK QTGGKVFVTS MCIGSGMGMA AVFVSEQ
//
