ID A0A0Q8QVI5_9SPHN Unreviewed; 390 AA.
AC A0A0Q8QVI5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRB85694.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRB85694.1};
GN ORFNames=ASE00_02645 {ECO:0000313|EMBL:KRB85694.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB85694.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB85694.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB85694.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB85694.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB85694.1,
RC ECO:0000313|Proteomes:UP000051854};
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:KRB85694.1}.
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DR EMBL; LMIB01000001; KRB85694.1; -; Genomic_DNA.
DR RefSeq; WP_056377571.1; NZ_LMIB01000001.1.
DR AlphaFoldDB; A0A0Q8QVI5; -.
DR STRING; 1736594.ASE00_02645; -.
DR OrthoDB; 7181944at2; -.
DR Proteomes; UP000051854; 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:KRB85694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRB85694.1}.
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; 39564 MW; E9FF5956839702EC CRC64;
MTDIVITGAK RTAVGSFLGA FASTPAHTLG QTAIIAALTQ AGVDAAEVQE AILGQVLSAG
QGQNPARQAA MNAGLPKEAT AFGVNQVCGS GLRAVALAAQ AIKCGDARVV VAGGQENMSL
SVHARALRAG AKMGDISLVD TMIVDGLTDV FNGYHMGITA ENLAEKYQIG RAEQDGFAVA
SQNKAEAAQA AGRFKDEIAP VTIKGRKGDT IVDQDEYIRA GATIEAMAGL KPAFKKDGTV
TAANASGIND GAAALVLMSA DDAAKRGAPV LGRIASWATC GVDPSIMGIG PAPASKLALE
KAGWKLSDLD LIEANEAFAA QALAVGKELG WNADIVNVNG GAIAIGHPIG ASGARVLTTL
LYEMGRRDAK KGLVTLCIGG GMGIAMCIER
//
