ID A4YEH9_METS5 Unreviewed; 395 AA.
AC A4YEH9;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABP94831.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ABP94831.1};
GN OrderedLocusNames=Msed_0656 {ECO:0000313|EMBL:ABP94831.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP94831.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP94831.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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DR EMBL; CP000682; ABP94831.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YEH9; -.
DR STRING; 399549.Msed_0656; -.
DR KEGG; mse:Msed_0656; -.
DR eggNOG; arCOG01282; Archaea.
DR HOGENOM; CLU_031026_0_0_2; -.
DR BioCyc; MetaCyc:MONOMER-13740; -.
DR BRENDA; 2.3.1.9; 7245.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase 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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ABP94831.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW Transferase {ECO:0000313|EMBL:ABP94831.1}.
FT DOMAIN 4..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 395 AA; 42989 MW; BAA22D75C948E5FA CRC64;
MPDVYIVSAV RTPIGRFGGS LKSVKPQMLG AIAIKEALRR ANTDPSRVEL TIMGNVLRSG
HGQDLARQAA LLAGIPWEVD GYCVDMVCSS GMMGVTNAAQ MIKSGDADVV VAGGMESMSQ
SMLAVNSEVR WGVKFLSGKS LNFIDTMLVD GLTDPFNLKL MGQEADMVAR ERDISRRELD
EVAFESHRRA HQAWEKGLFK SEVIPVNLDE GKLERDEGIR PDTTMEKLSS LKPAFTENGY
HTAGNSSQIS DGAVAMVLMS EKAVKEFGVD PVAKILGYSW VGIESWRFTE APLYSVRKLL
TRLNMNITQF DYFENNEAFA VNNVLFHRYL GVPYDQLNVF GGAIALGHPI GASGARIMVT
LLNVLSKMNA TRGIASICHG VGGSTAIALE LLRPL
//
