ID A0A094D3D7_9PEZI Unreviewed; 628 AA.
AC A0A094D3D7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=V497_03234 {ECO:0000313|EMBL:KFY60926.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY60926.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY60926.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY60926.1}.
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DR EMBL; JPJZ01000771; KFY60926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094D3D7; -.
DR STRING; 1420910.A0A094D3D7; -.
DR HOGENOM; CLU_398022_0_0_1; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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; IPR020610; Thiolase_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 SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268}.
FT DOMAIN 41..297
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"
SQ SEQUENCE 628 AA; 65873 MW; 0522C08EB85B6A61 CRC64;
MSVRMAMSSL QASRASSQRV AQVSRHFSTT GAARQEIQDA YIISASRTPT AKFNGSFLTV
PAPKLGAVAI KSALEKSKVP VSKITDVYMG NVLQGGVGQA PARQAAIFAG LPTSVEAITI
NKVCASGMKA VVFAAQNIQL GLAEAQIAGG MENMSRVPSY LPRASSQPAF GNQQIKDGLI
EDGLWDVYNQ FHMGVCAETT AKKYNITREQ QDEYAVQSYK RAQDAWKNQA FKEEIAPVTV
TGRKGDIIID TDEGYLDIKP EKIATLKPAF IRDGTGTVTA ANASTFNDGA SALVLGNKEI
AREYGSGSRV LARICGTADA AMDPVDFPIA PAKAVPIALE RAGITKDQVA VWEFNEAFAA
VIKANEQILG LEGKRVNELG GAISLGHALG SSGSRIIVTL LHQLKVGEYG VAAICNGGGA
ATAIVVQRID KSAGVALQER ALPRASKILN AGDQLAGVVP AVLVDLLDGV GDVLEGAGAA
AEGAAAAVDT EAAGLEVEGC GVQVDGCGGD GGCCKEQGGE DGARTEVHLG HHENNQSCFG
MGKLKAIISH PAIPTRQASS RARHKHNPPA LFSYDDADYG RSALTTGLLF RCSALPVLAL
LRLPLVVKAP EFGQSLRDLW ALEQIFER
//