ID A0A223CX24_9BACL Unreviewed; 394 AA.
AC A0A223CX24;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN ORFNames=CIG75_01905 {ECO:0000313|EMBL:ASS73848.1};
OS Tumebacillus algifaecis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS73848.1, ECO:0000313|Proteomes:UP000214688};
RN [1] {ECO:0000313|EMBL:ASS73848.1, ECO:0000313|Proteomes:UP000214688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THMBR28 {ECO:0000313|EMBL:ASS73848.1,
RC ECO:0000313|Proteomes:UP000214688};
RX PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
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; CP022657; ASS73848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223CX24; -.
DR KEGG; tab:CIG75_01905; -.
DR OrthoDB; 2379477at2; -.
DR Proteomes; UP000214688; 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; 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; 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; 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:ASS73848.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000214688};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ASS73848.1}.
FT DOMAIN 7..265
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..394
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 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40963 MW; 04BB2FDBC03ADF2D CRC64;
MANRDAVIVS AVRTAIGNFQ GALAGIPAPE LGAVVLTAAL ERAGVSADLV EEVILGNVLQ
AGLGQNPARQ AAIKAGLPNT IASMTINKVC GSGLKAVMLA AQAIKAGDAD VILAGGFENM
SRAPYLLEGA RTGYRMGDQK VTDIMIRDGL WCAFDDTHMG ITAENVAERY GLTREEQDEF
AAWSQQKAEA ALASDRFKDE IVPVQIPQRK GDPIVFDKDE FPRAGTTAAS LGKLRPAFKK
EGTVTAGNAS GINDGAAAVL VMSREKAEAL GLKILGTVTA YASAGLDPNV MGLGPIYATK
KVLDRAGLSI GDIDLIEANE AFAAQSLAVG RDLEIPREKL NVNGGAIALG HPIGASGTRV
LVSLIHEMEK QEAKRGLATL CIGGGQGVAL VIER
//
