ID A0A142L273_9BACT Unreviewed; 390 AA.
AC A0A142L273;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=AEM51_04055 {ECO:0000313|EMBL:AMS26319.1};
OS Bacteroidetes bacterium UKL13-3.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1690483 {ECO:0000313|EMBL:AMS26319.1, ECO:0000313|Proteomes:UP000075224};
RN [1] {ECO:0000313|Proteomes:UP000075224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP012155; AMS26319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142L273; -.
DR STRING; 1690483.AEM51_04055; -.
DR KEGG; bbau:AEM51_04055; -.
DR PATRIC; fig|1690483.4.peg.862; -.
DR Proteomes; UP000075224; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:AMS26319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075224};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AMS26319.1}.
FT DOMAIN 4..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 267..387
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 41622 MW; BE682AEF32411A37 CRC64;
MNAYIIKGFR TAVGKANKGG FRFTRPDDLA AEVIKYLVAA VPELDPSRVD DLIVGNAVPE
AEQGMQMGRM ISLLSLPIKV PGMVVNRYCG SGLETIAMAS AKIHAGMADC IIAGGTESMS
LVPTIGWKTV LNYDIAKSHP DWYSSMGATA ESVASEYNVS REDQDAFAFA SHQKALAAIN
EGKFKNQIVP VTVKETYIDE KGKRKTRDFV VDTDEGPRAD TSLQGLAKLK PVFKNGGSVT
AGNSSQTSDG ASFVIVMSER MVNELNLKPI ARMVSYAVSG VEPRIMGIGP VEAIPLALKQ
AGLSLNQIQQ IELNEAFAAQ SLAVMRQLNI DPEIVNVNGG AIALGHPLGC SGAKLSVQLW
DEMRRRNQQY GIVSACVGGG QGVAGVYELL
//
