ID A0A0Q8RJG3_9SPHN Unreviewed; 390 AA.
AC A0A0Q8RJG3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRB94567.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRB94567.1};
GN ORFNames=ASE22_01070 {ECO:0000313|EMBL:KRB94567.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB94567.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB94567.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB94567.1,
RC ECO:0000313|Proteomes:UP000051570};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB94567.1}.
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DR EMBL; LMID01000001; KRB94567.1; -; Genomic_DNA.
DR RefSeq; WP_056353785.1; NZ_LMID01000001.1.
DR AlphaFoldDB; A0A0Q8RJG3; -.
DR STRING; 1736595.ASE22_01070; -.
DR Proteomes; UP000051570; 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; 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 ECO:0000313|EMBL:KRB94567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051570};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRB94567.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 39787 MW; 23EA1E8E82B5F0DF CRC64;
MTDIVIVGAK RTPVGSFLGA FAATPAHELG RTAIEASLAQ AGVEAGEVQE AILGQVLTAG
QGQNPARQAA INAGIPKEAT AFGVNQVCGS GLRAVALAAQ SIRCGDARVV VAGGQESMSL
SMHAQNLRGG FKMGNASLVD TMIVDGLTDA FNAYHMGITA ENLAEKYQIG RAEQDAFAVA
SQNKAETAQT AGRFDDEIAA VTVKGRKGDT IVSRDEYIRA GATIEAMAGL KPAFKKDGTV
TAANASGLND GAAALVLMTA NDAAKRGAPI LGRIASWATC GVDPSIMGIG PAPASRLALE
KAGWKLSDLD LIEANEAFAA QALAVGKELG WNTDIVNVNG GAIAIGHPIG ASGARVLTTL
LYEMAKRDAK KGLVTLCIGG GMGIAMCIER
//
