ID A0A2D1SP93_9BACL Unreviewed; 400 AA.
AC A0A2D1SP93;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CSE16_02295 {ECO:0000313|EMBL:ATP38942.1};
OS Solibacillus sp. R5-41.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=2048654 {ECO:0000313|EMBL:ATP38942.1, ECO:0000313|Proteomes:UP000222866};
RN [1] {ECO:0000313|EMBL:ATP38942.1, ECO:0000313|Proteomes:UP000222866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5-41 {ECO:0000313|EMBL:ATP38942.1,
RC ECO:0000313|Proteomes:UP000222866};
RA Guo Y., Chen Z., Wang H.;
RT "Complete genome sequence of Solibacillus sp. R5-41.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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; CP024123; ATP38942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D1SP93; -.
DR KEGG; sob:CSE16_02295; -.
DR OrthoDB; 2774224at2; -.
DR Proteomes; UP000222866; 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:ATP38942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000222866};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ATP38942.1}.
FT DOMAIN 5..265
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
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 400 AA; 41822 MW; 95FF53847A0D683F CRC64;
MSKTVILDGA RTAFGKFGGV LGSLSASDLG GIAIAEALKK ADVAVDDVQE VIIGNVLQAG
QGQIPSRQAA TKAGIPWHVK TETINKVCAS GMRSVTLADQ LIRSGDEEII VAGGMESMSN
APYYMPKGRF GLRMGDATLV DGLLHDGLTC AFNPQQVHMG VYGNETAQQF QISRELQDAW
AVRSHERAIA AIEDGKFAQE IAVVELAQRK GEPIRIEQDE APRKGTSMEA LSKLKSAFSQ
DGTITAGNAP GVNDGACALV LMSEERAQKE NRQPLAKILA HAEVGVAPEQ FPQTPGLVIN
ALLEKTGKSL EEIDLVEINE AFAAVALVSN ELATLDAEKV NVNGGAVALG HPIGASGARI
ILTLAYELKR RGGGLGIAAI CSGGGQGDAI LIEVPGKGEK
//
