ID A0A1I6C6J9_9BACI Unreviewed; 395 AA.
AC A0A1I6C6J9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN04488577_3322 {ECO:0000313|EMBL:SFQ88802.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ88802.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ88802.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ88802.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOYF01000005; SFQ88802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6C6J9; -.
DR STRING; 1761761.SAMN04488577_3322; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000199578; Unassembled WGS sequence.
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; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000199578};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SFQ88802.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..391
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 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 395 AA; 41489 MW; 2DEEAB132E909E64 CRC64;
MGRTVILSGV RTPFGKFGGS LSSFSASELG GMAVKEALNR ADIKPEEVNE VILGSVLQGG
QGQIPSRQAA KHAGLPWEVK TETINKVCAS GMRSVTLADQ IIRAGDEEVI VAGGMESMSN
APYLLPKARW GLRMGDSSVK DLMVYDGLTC TFTGVHMGTY GNSTAKEMEI SREEQDRWAA
RSHERVIAAI EAGKLAEEIV PVSVPQRKGD PIVVEHDESP RKDTSFEKLS KLGVVFNSDG
TITAGNAPGI NDGAAALVLM SEERAEKEGR KAEAYILAHE AIAVEAKDFP KTPGLVINAL
LKKAGKTLDE INLFEINEAF AAVALASGKI AGLDPEKVNV NGGAVAIGHP IGASGARIII
TLMHELKRRG GGIGIAAICS GGGQGDAIMI EVPKA
//
