ID A0A1H9ZAD2_9BACI Unreviewed; 397 AA.
AC A0A1H9ZAD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05421676_101426 {ECO:0000313|EMBL:SES77807.1};
OS Salinibacillus kushneri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX NCBI_TaxID=237682 {ECO:0000313|EMBL:SES77807.1, ECO:0000313|Proteomes:UP000199095};
RN [1] {ECO:0000313|EMBL:SES77807.1, ECO:0000313|Proteomes:UP000199095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SES77807.1,
RC ECO:0000313|Proteomes:UP000199095};
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; FOHJ01000001; SES77807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9ZAD2; -.
DR STRING; 237682.SAMN05421676_101426; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000199095; 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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SES77807.1}.
FT DOMAIN 7..265
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 274..394
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 397 AA; 42639 MW; 4489E69FBDD5A457 CRC64;
MELKESYIIG SVRTAVGKMG GALQDVTADY LGEKVIREVL NRYGNEVEVD EVILGQAKQS
QDQANLGRLS ALRAGLPVSV SGYTVHRQCG SGLQAINNAD MQLKLGLSDV VVAGGAESMS
TAPFYLRNAR YGYKAGNGVL VDPNTESQPC SQPREEYGEL TMGLTAENLA EKYQISREEQ
DAFAQRSQEL ADKAIQEGRF KDEIVPFEVK MRKNTFTFDT DEHPRLTSLE KLSKLPAVFK
EGGTVTPGNA SGRNDGAAAL LMMNKEKADE YGIKPQARII AQATSGVSPD IMGIGPVEST
AKALKQADLS IDDIGIIELN EAFAAQSIAV IREAKMDLNR VNVNGGAIAL GHPIGATGAI
ITTKLLHEME KRGEKYGLVT LCIGGGQGIS TIIEYLQ
//
