ID   A0A0G1MAH3_9BACT        Unreviewed;       817 AA.
AC   A0A0G1MAH3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KKU05271.1};
GN   ORFNames=UX07_C0019G0003 {ECO:0000313|EMBL:KKU05271.1};
OS   Parcubacteria group bacterium GW2011_GWA2_45_30.
OC   Bacteria.
OX   NCBI_TaxID=1618834 {ECO:0000313|EMBL:KKU05271.1, ECO:0000313|Proteomes:UP000033829};
RN   [1] {ECO:0000313|EMBL:KKU05271.1, ECO:0000313|Proteomes:UP000033829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKU05271.1}.
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DR   EMBL; LCKU01000019; KKU05271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1MAH3; -.
DR   Proteomes; UP000033829; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:KKU05271.1}.
FT   DOMAIN          6..269
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          277..397
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   DOMAIN          416..595
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          598..693
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          725..806
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   817 AA;  89723 MW;  2E248CFB59297EF3 CRC64;
     MALEKIVIVE AGRTPSGKHM GAFRDIPAEN LLAECYKWII AQSNINPNLI DEIIASNCYT
     KSSAPNIAHV AARIAGLPSQ IPAWTPMNNC GSGTKAIISA YQAIRVGDYK IILVGGTENM
     SEVPRYETKS RLGPKFGNIV LVDSLTEGLA DSLALDEITG TKALYWQIAE NSIRKHKISR
     KNQDEWAVIS HQRAHRATNE GLFRPRMIPI NNHMADETIN TALVKNPQLA SGFPDLLGHL
     FQKEGGTVTP ANSSQISDGA GTLLIMLESR ARTLGLNPLA EIVAYASAGG DPLFMGELPV
     KAILKTLEKA GLTAKDVDFL QLNEAFSGQT LACIKQLPFT EDQVNPNGGA IALGHPLGAS
     GIMRTVDSIT ILENTDARYV MTAFCIGGGQ GIALLLKRPE TLIKRKPASE RIISEVGIIG
     GAGTMGHGIS IWLARQGIPV TMLEGTPELS VKARQLLDER IDGYVERGII AKAEADHQKS
     LVVSSHDMES LKDCDLVMEA APENMKLKKK IFRELDKIMK PGAILASNTS SLSITDLGAE
     TGRPDKIIGV HWFNPPWKMK LVEIVVGKET SEETYKRVRR FVQEQSQKTP IHVKDSPGFY
     VNRALAALLL EGVNNLMRYR FDIKALDTRM KETGWPATGC FWLLDWLGLP LVKDVLLVLE
     KAFGQRMQTP KLLSCMTDEG RLGERWSAGF YDYGATAQHK SLEEILESNF PERPEEDLEK
     IYYLMMCQFV NESARCLEEG IISLDDIGAG ACLGIGFPFG LEHPLKWADK EGLSEIVKAL
     SAAHKKTGDP RYAISVLLHE NAKAEKNFFG SQDKLEW
//