ID K6E8M6_9BACI Unreviewed; 395 AA.
AC K6E8M6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=BABA_09676 {ECO:0000313|EMBL:EKN69686.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN69686.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN69686.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN69686.1}.
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DR EMBL; AJLS01000055; EKN69686.1; -; Genomic_DNA.
DR RefSeq; WP_007084954.1; NZ_AJLS01000055.1.
DR AlphaFoldDB; K6E8M6; -.
DR STRING; 1117379.BABA_09676; -.
DR PATRIC; fig|1117379.3.peg.2019; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000006316; 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:UP000006316};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EKN69686.1}.
FT DOMAIN 6..265
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..393
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 395 AA; 41261 MW; 211126B1E3B72BDA CRC64;
MSQKEVVIVG AVRTALGNFN GGLKNVSAPD LGATVIKGAL EHAGVKPDQV DEVIMGNVLQ
AGLGQNPARQ AAMKAGIPET ASSMTINKVC GSGLKAVHLA TQAILAGDAE IIVAGGMENM
SQAPYLLKNA RDGFKMGDQK LVDTLTSDGL TCIFNDYHMG ITAENLAEKY SITREEQDEF
SAWSQDKAVK AIENGRFKDE IVPVVIPQRK GEPIVFEIDE YPKKGTTAEK LAGLRPAFKK
DGSVTAGNAS GINDGAAAVV VMSKEKADEL GLKPLVTIKA NTSAGVDPSI MGIGPVPAVR
KALEKASVSI EDLNLIEANE AFAAQSLAVD RELHLNKEIL NVNGGAIALG HPIGASGARI
LVTLIHEMKR RNAQTGLATL CIGGGQGVAT IVELV
//
