ID A0A3A9SNZ4_9FIRM Unreviewed; 392 AA.
AC A0A3A9SNZ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=D6855_07160 {ECO:0000313|EMBL:RKM60488.1};
OS Butyrivibrio sp. CB08.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=2364879 {ECO:0000313|EMBL:RKM60488.1, ECO:0000313|Proteomes:UP000281491};
RN [1] {ECO:0000313|Proteomes:UP000281491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB08 {ECO:0000313|Proteomes:UP000281491};
RA Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
RL Submitted (SEP-2018) 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:RKM60488.1}.
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DR EMBL; RAIR01000003; RKM60488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9SNZ4; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000281491; 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:UP000281491};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RKM60488.1}.
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 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 392 AA; 40726 MW; 1B3D80BBC3EAEF13 CRC64;
MARKVVLAGA CRTAIGTMGG ALSTTPAPVL GGIVIKEALN RAGIKPEQVD EVYMGCVIQA
GLGQNAARQA SINAGIPVEV PATTINVLCG SGLHSVNLAA KLVAVGDADI IVAGGMENMS
MAPYLVKQGR YGYRMGTGAL EDALIHDGLT DAFGGYHMGI TAENIAEQWH LTRQQLDEFA
AWSQNKAEKA IAEGKFKDEI VPVEVKKKKE TIIFDTDEGP RSGVTVEGIS HLKPAFKKDG
VVTAANSSGI NDAASAIIVM SEEKAKELGV KPMATWIAGA LAGVEPSIMG IGPVAATQKV
MKKAGYSIGD FDLIEANEAF AAQSIAVQHD LGFSNEVLNV NGGAIALGHP VGCSGNRILV
SLLYEMQRRD AKKGLATLCV GGGMGCAAIV ER
//