ID A0A0A8X0A8_9BACI Unreviewed; 389 AA.
AC A0A0A8X0A8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SAMD00020551_1490 {ECO:0000313|EMBL:GAM13348.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM13348.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM13348.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM13348.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAM13348.1}.
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DR EMBL; BASE01000031; GAM13348.1; -; Genomic_DNA.
DR RefSeq; WP_041965204.1; NZ_BASE01000031.1.
DR AlphaFoldDB; A0A0A8X0A8; -.
DR STRING; 1321606.SAMD00020551_1490; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000031014; Unassembled WGS sequence.
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; 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; 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:GAM13348.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031014};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:GAM13348.1}.
FT DOMAIN 6..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 267..388
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 126..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 389 AA; 40995 MW; 84A5CDE8150D5DF8 CRC64;
MNRNAVIVSA VRTAIGRQGG ALASVPAHVF GAEVINEAIR RANVQPEMIE DVIMGNVISG
GGNIARLTAL QTGLSLALPG LTIDRQCGSG INAVNLAAQA IKAGAGDVYV AGGIESMSRA
PYLMDKPERP YSPVPPSFRK SQLSPKEIGD PPMGITAENL VKKYSISREE QDEFALSSQQ
KMAAAMSEGR FDEQIVPITI PVRKGIPVIF NKDEHPRPQT TMETLAQLKP AFLPNGTVTA
GSSSGLNDAA AALMVMSREK AQELGVKPMA VVREQAVAGV DPKIMGIGPV PAVRKVLEKS
GLTLDDMDFI EINEAFAAQV IACDRELTMD KAKVNVNGGA IAHGHPLGAT GAILITKAVY
ELERRGGRYA LITACIGGGQ GIATIIERE
//
