ID A0A1H7RK44_9SPHI Unreviewed; 391 AA.
AC A0A1H7RK44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=SAMN05421740_107165 {ECO:0000313|EMBL:SEL60601.1};
OS Parapedobacter koreensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=332977 {ECO:0000313|EMBL:SEL60601.1, ECO:0000313|Proteomes:UP000198916};
RN [1] {ECO:0000313|EMBL:SEL60601.1, ECO:0000313|Proteomes:UP000198916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip14 {ECO:0000313|EMBL:SEL60601.1,
RC ECO:0000313|Proteomes:UP000198916};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNZR01000007; SEL60601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7RK44; -.
DR STRING; 332977.SAMN05421740_107165; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000198916; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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:SEL60601.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SEL60601.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 41373 MW; 94D103B46ECC5968 CRC64;
MEAYIIAGFR TAVGKAPRGV FRFTRADDLA AAVIKHLVAS VPNLDNEQID DVIVGNATPE
AEQGLNVGRL ISLMGLDTDK VPGVTVNRYC ASGLETIATA VAKIKAGMAD TIIAGGVEVM
SGMPMGGWKL VPNPEVAKHH PDWYWNMGLT AEAVAKEYKV SREDQDAFAF QSHQKAITGI
QNGNLKDGVV PITVAERYLE DGKKIKTREY VVDTDEGPRA DTSPEALAKL RPVFAAGGSV
TAGNSSQTSD GAAFVLVVSE RKLKELGVQP IARLVSYGVA GVPPRIMGIG PIFAIPKALG
MAGMKLDEID LIELNEAFAS QSLAVVRKLG INPDILNVNG GAIALGHPLG CTGAKLSVQL
FHELKRRNQK YGMVTMCVGT GQGAAGIFEL L
//
