ID A0A0Q6ZB91_9BRAD Unreviewed; 391 AA.
AC A0A0Q6ZB91;
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:KQW19278.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KQW19278.1};
GN ORFNames=ASC80_17870 {ECO:0000313|EMBL:KQW19278.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW19278.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW19278.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW19278.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW19278.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW19278.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW19278.1}.
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DR EMBL; LMDP01000003; KQW19278.1; -; Genomic_DNA.
DR RefSeq; WP_056300050.1; NZ_LMDP01000003.1.
DR AlphaFoldDB; A0A0Q6ZB91; -.
DR STRING; 1736436.ASC80_17870; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000051348; 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:KQW19278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQW19278.1}.
FT DOMAIN 5..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..391
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 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40562 MW; D5F4E2F98BF17D23 CRC64;
MSDDVVIVSA ARTAVGSFNG AFANTPAHEL GAVAIKAALE RAGIEPARVS EIIMGQILTA
AQGQNPARQA AMKAGIPVES PAWGINQLCG SGLRTVALGY QALMNGDSEI VVAGGQESMS
MAPHAQHLRG GVKMGAFDLV DTMIKDGLWD AFNGYHMGNT AENVARQFQI TRQQQDEFAV
KSQNKAEAAQ KAGKFKDEIV PFTVKTRKGE VVVDADEGPR HGASVDAMAK LRPAFEKEGT
VTAGNASTIN DGAAALVLMT AKQAAKEGKT PLARIVSWAQ AGVDPSIMGT GPIPASRAAL
KKAGWKPGDL DLIEANEAFA AQASAVNKEI GWDPAKVNVN GGAIAIGHPI GASGARVLVT
LLHEMQKRDA KKGLATLCIG GGMGIALCVE R
//
