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Database: UniProt
Entry: A0A3A9SNZ4_9FIRM
LinkDB: A0A3A9SNZ4_9FIRM
Original site: A0A3A9SNZ4_9FIRM 
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
//
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