ID A0A365L1A5_9BACL Unreviewed; 394 AA.
AC A0A365L1A5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN ORFNames=DP120_05920 {ECO:0000313|EMBL:RAZ79153.1};
OS Planococcus halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=2233542 {ECO:0000313|EMBL:RAZ79153.1, ECO:0000313|Proteomes:UP000251002};
RN [1] {ECO:0000313|EMBL:RAZ79153.1, ECO:0000313|Proteomes:UP000251002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCU63 {ECO:0000313|EMBL:RAZ79153.1,
RC ECO:0000313|Proteomes:UP000251002};
RA Gan L.;
RT "The draft genome sequences of strains SCU63 and S1.";
RL Submitted (JUN-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:RAZ79153.1}.
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DR EMBL; QLZR01000002; RAZ79153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365L1A5; -.
DR Proteomes; UP000251002; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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:SF164; ACETYL-COA ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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 ECO:0000313|EMBL:RAZ79153.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000251002};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RAZ79153.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..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 394 AA; 41007 MW; E4EE006FE20F8113 CRC64;
MSQEIVIVSA VRTAVGSFQG SLKDVPATEL GAIVIKEAVK RAGIEPAQVS EVIMGNVLQA
GLGQNPARQA AMGAGLPETV PSMTINKVCG SGLKSIHLAY QAIFAGDAEI VVAGGMENMS
RAPYLLENAR GGFRMGDQKV VDSMVSDGLT CAFNDYHMGN TAENLCDRYG ISREEQDKFA
ARSQARAAAA VEAGKFHEEI VPVEIPQRKG DPIIFAEDEY IKASSTEEKL GKLRPAFKKD
GSVTAGNASG INDGAAAVVV MTKAKAEELG LTVLATIAAN GNAGVDPAVM GIGPVQAVKN
ALAKAAMSLE DIELIEANEA FAAQSIAVDR ELKFNHDILN VNGGAIAIGH PIGASGTRIF
VTLLHEMQKR DAKTGLATLC IGGGQGVATI VKRP
//
