ID A0A0R2LPU7_9LACO Unreviewed; 388 AA.
AC A0A0R2LPU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=IV54_GL000225 {ECO:0000313|EMBL:KRO03433.1};
OS Levilactobacillus paucivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=616990 {ECO:0000313|EMBL:KRO03433.1, ECO:0000313|Proteomes:UP000051906};
RN [1] {ECO:0000313|EMBL:KRO03433.1, ECO:0000313|Proteomes:UP000051906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22467 {ECO:0000313|EMBL:KRO03433.1,
RC ECO:0000313|Proteomes:UP000051906};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRO03433.1}.
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DR EMBL; JQCA01000094; KRO03433.1; -; Genomic_DNA.
DR RefSeq; WP_057878796.1; NZ_JQCA01000094.1.
DR AlphaFoldDB; A0A0R2LPU7; -.
DR STRING; 616990.IV54_GL000225; -.
DR PATRIC; fig|616990.3.peg.247; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000051906; 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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRO03433.1}.
FT DOMAIN 5..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..388
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 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 388 AA; 40789 MW; AF34B1BAD5CB9DA9 CRC64;
MAEEVVIVSA VRTPIGKFGR NFRSVSAVTL GTIAAKAAIK RSGLEPNMIQ QTIFGTVLQA
GQGQNVARQI ELNAGLPASS TAMTVNQVCG SSLKAIRLGQ GAILMGDADA VLVGGTESMS
RAPYLSHHAR WGRKFGDLTL TDSLAKDGLT DAFSQVPMGI TVENVAEKFN VSRADQDAFA
LRSQQKATQA QADHHFDAEI VPVPVDGKTI TQDEAVRTTT SLDQLEALKP AFKTNGTVTA
GNAAGLNDGA AAMVLMRKSA AIAAGIPYLA TLSGYQESGI DPQIMGYAPV TAIQKVLRDH
HLTVADIDRF EINEAFAAQS VAITRDLQIP ADRLNVNGGS IALGHPLGAS GTRIVVTLLH
ELLRTQTHRG LAAMCIGGGM GMTLLVER
//