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Database: UniProt
Entry: Q4JA55_SULAC
LinkDB: Q4JA55_SULAC
Original site: Q4JA55_SULAC 
ID   Q4JA55_SULAC            Unreviewed;       392 AA.
AC   Q4JA55;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AAY80325.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:AAY80325.1};
GN   OrderedLocusNames=Saci_0963 {ECO:0000313|EMBL:AAY80325.1};
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY80325.1, ECO:0000313|Proteomes:UP000001018};
RN   [1] {ECO:0000313|EMBL:AAY80325.1, ECO:0000313|Proteomes:UP000001018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
RC   {ECO:0000313|Proteomes:UP000001018};
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982}.
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DR   EMBL; CP000077; AAY80325.1; -; Genomic_DNA.
DR   RefSeq; WP_011277827.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4JA55; -.
DR   STRING; 330779.Saci_0963; -.
DR   GeneID; 78441310; -.
DR   KEGG; sai:Saci_0963; -.
DR   PATRIC; fig|330779.12.peg.924; -.
DR   eggNOG; arCOG01282; Archaea.
DR   HOGENOM; CLU_031026_0_0_2; -.
DR   Proteomes; UP000001018; 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:AAY80325.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001018};
KW   Transferase {ECO:0000313|EMBL:AAY80325.1}.
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   392 AA;  42551 MW;  9BD8667BEE3D02F5 CRC64;
     MDNVYIVSAV RTPLGKFGGS LKDISPSELG SVVIREAVNR AKVDPKLIDI VIMGNVLRAG
     HGQDLARQAS IKAGIPAKTD AYCVDMVCSS GMISTINAVQ MIKSEDADIV VAGGMESMSR
     ASFAIGSEIR WGTKMLMNKS LDIIDTMIID GLTDPFNFKV MGQEADMVAR EHEITRRELD
     EVAYESHRRA TIATEKGYFK DEIVPLNVDG RVVDKDEGIR ADTTLEKLLQ LKPAFGSDGL
     HTAGNSSQIS DGAAALVFVS ESAVRKFKLE PIARVLGYSW IGIESWKFPE APIYSVKKLL
     DKINIPLSKF DYFENNEAFA VNNVLFNRYL GVSYDRLNVY GGAIALGHPI GASGSRILVT
     LLNVLRKMNG KYGIASICHG IGGSTAIAVE LL
//
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