ID G3ALB7_SPAPN Unreviewed; 404 AA.
AC G3ALB7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=SPAPADRAFT_60466 {ECO:0000313|EMBL:EGW33160.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW33160.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC {ECO:0000256|ARBA:ARBA00037924}.
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; GL996501; EGW33160.1; -; Genomic_DNA.
DR RefSeq; XP_007374675.1; XM_007374613.1.
DR AlphaFoldDB; G3ALB7; -.
DR STRING; 619300.G3ALB7; -.
DR GeneID; 18873427; -.
DR KEGG; spaa:SPAPADRAFT_60466; -.
DR eggNOG; KOG1390; Eukaryota.
DR HOGENOM; CLU_031026_0_0_1; -.
DR InParanoid; G3ALB7; -.
DR OMA; ICPSIAI; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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; 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; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 6..266
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 274..396
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 404 AA; 41887 MW; E2CA38CE7785FC8F CRC64;
MTVPPVYIVS AARTPVGSFQ GQLSSLSYSD LGAHAVKAAL AKVPQIQPSE VDEIVFGGVL
QANVGQAPAR QVALKAGLPN SIVASTINKV CASGMKSIII GAQNIICGTS EIVVAGGAES
MSNTPYYLPA ARTGARYGDS VMVDGVQKDG LLDVYEQKLM GVAAEKCAKD HGFTRDDQDD
FAVGSYKKAA EAYAQGKFAS EVAPITIKGI RGKPDVVVSE DEEVKNLNES RLRSARTVFQ
KENGTVTAPN ASKLNDGGAA VVLVSEAKLK QLGLKPIAKI VGWGEAATEP FDFTIAPSLA
VPKALKHANV SLDQVDYFEL NEAFSVVGLA NTKLLNLPAD RVNVYGGAVA IGHPLGCSGA
RIVVTLLSIL GQEGGKIGVA GICNGGGGAS SIVIEKLDHD ESKL
//