ID F2KP59_ARCVS Unreviewed; 422 AA.
AC F2KP59;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AEA47463.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:AEA47463.1};
GN OrderedLocusNames=Arcve_1460 {ECO:0000313|EMBL:AEA47463.1};
OS Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA47463.1, ECO:0000313|Proteomes:UP000008136};
RN [1] {ECO:0000313|EMBL:AEA47463.1, ECO:0000313|Proteomes:UP000008136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNP6;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Archaeoglobus veneficus SNP6.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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DR EMBL; CP002588; AEA47463.1; -; Genomic_DNA.
DR RefSeq; WP_013684124.1; NC_015320.1.
DR AlphaFoldDB; F2KP59; -.
DR STRING; 693661.Arcve_1460; -.
DR GeneID; 10394584; -.
DR KEGG; ave:Arcve_1460; -.
DR eggNOG; arCOG01282; Archaea.
DR HOGENOM; CLU_031026_0_0_2; -.
DR OrthoDB; 25212at2157; -.
DR Proteomes; UP000008136; 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; -; 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; 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; 2.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 2.
DR SUPFAM; SSF53901; Thiolase-like; 3.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AEA47463.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008136};
KW Transferase {ECO:0000313|EMBL:AEA47463.1}.
FT DOMAIN 4..45
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 75..290
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 297..418
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 422 AA; 45524 MW; F00463E1E38AC7F9 CRC64;
MDAVVVGAVR TPVGRFGGAL KDFQAYELGA IAIKGLLKKL NLKPISSQEE YPSKLHKGRI
DLEEKYYDYD GIEIEIDEVI MGNVLQAAQG QNPARQAAIF AGIPKEVPAF TVNMVCGSGL
KAVALAAQSI AIGESDVIVA GGMESMSNAP YALTKARWGY RMFNGELLDL MVHDGLWEKF
YGYHMGVTAE NIVELYGISR EEQDRLAYES HMRAVKAIDE GIFREEIVPV TVQTKVGTVT
IDTDEHPRRD TSIEKLAKLP PVFKKDGTIT AGNASGVNDG AAALILMSEE KAKELNLKPM
ARIVSYACAA IDPAYMGLAP IPAIKKAVKK AGLSIEEIDL IELNEAFAAQ AIAVMKELNL
DPEKTNVHGS GISLGHPIGA TGARITTTLL HEMQRRKAKY GLSALCIGGG MGIAMVFESY
SH
//