ID A0A2A9CI84_9BACI Unreviewed; 396 AA.
AC A0A2A9CI84;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=ATG70_1544 {ECO:0000313|EMBL:PFG13342.1};
OS Bacillus sp. es.036.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761764 {ECO:0000313|EMBL:PFG13342.1, ECO:0000313|Proteomes:UP000222003};
RN [1] {ECO:0000313|EMBL:PFG13342.1, ECO:0000313|Proteomes:UP000222003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=es.036 {ECO:0000313|Proteomes:UP000222003};
RA Fredrickson J.;
RT "Microbial Interactions in Extremophilic Mat Communities.";
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}.
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:PFG13342.1}.
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DR EMBL; PDIZ01000001; PFG13342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9CI84; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000222003; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PFG13342.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
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 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 396 AA; 42145 MW; CFC8A0341A4EA74A CRC64;
MSENIVIVEA VRTPVGRYGG VLKNFNSGEL AAIAIKETIA RAGITPELID EVILGEVRQT
TESSNVARVA ALRAGVSAAS PAFTINRLCA SGMQAIASAV QQIHSRQAEI LIAGGTESLS
NAPIYLRNSR IGGDKTTLID SNLEAGQQPV ELYGNHLGMG ITAENVAEKY QISREDQDAF
AAESQRRAAV AIENNVFAEE IVPVEAKSRR QTNLVNHDEH PRPGTTIEKL SMLKPVFKED
GSVTAGNSCG RNDGAVAMLV MTEAKARELQ LQPLARIIDW ATSGISPEIM GVGPVPAVKK
LLERTGKQLN DIGLIELNEA FAAQALAVIR ELGLQSDKVN VNGGAIALGH PLGATGARIL
TSLMYEMKRR DERFGIATLC VGGGQGMAMM VENMVN
//
