ID A0A0Q4VMN1_9RHIZ Unreviewed; 393 AA. AC A0A0Q4VMN1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-AUG-2020, entry version 17. DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQO73777.1}; DE EC=2.3.1.9 {ECO:0000313|EMBL:KQO73777.1}; GN ORFNames=ASF29_15230 {ECO:0000313|EMBL:KQO73777.1}; OS Rhizobium sp. Leaf262. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; OC Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736312 {ECO:0000313|EMBL:KQO73777.1, ECO:0000313|Proteomes:UP000052131}; RN [1] {ECO:0000313|EMBL:KQO73777.1, ECO:0000313|Proteomes:UP000052131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf262 {ECO:0000313|EMBL:KQO73777.1, RC ECO:0000313|Proteomes:UP000052131}; RA Gilbert D.G.; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQO73777.1, ECO:0000313|Proteomes:UP000052131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf262 {ECO:0000313|EMBL:KQO73777.1, RC ECO:0000313|Proteomes:UP000052131}; 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:KQO73777.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LMMM01000021; KQO73777.1; -; Genomic_DNA. DR RefSeq; WP_062452952.1; NZ_LMMM01000021.1. DR EnsemblBacteria; KQO73777; KQO73777; ASF29_15230. DR Proteomes; UP000052131; 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 Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1. 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:KQO73777.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557, KW ECO:0000313|EMBL:KQO73777.1}. FT DOMAIN 6..262 FT /note="Thiolase_N" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 271..391 FT /note="Thiolase_C" FT /evidence="ECO:0000259|Pfam:PF02803" FT ACT_SITE 90 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1" FT ACT_SITE 349 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1" FT ACT_SITE 379 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1" SQ SEQUENCE 393 AA; 40623 MW; 40521AF94FD0D2DC CRC64; MASTSIVIVS AARTAVGSFN GSFANTPAHE LGAAAITAVL DRSGIQSNEV DEVILGQILT AGAGQNPARQ AAMQAGIPQE ATAFGINQLC GSGLRAIALG MQQIATGDAS IIVAGGQESM SMAPHCAHLR GGVKMGDFTM TDTMLKDGLT DAFYGYHMGI TAENIVSKWQ LSREEQDQFA VTSQNRAESA QSGGRFVNEI VPFTIKGRKG DVSLDKDEYI RAGVSLDMLS KLRPAFDKNG TVTAGNASGL NDGAAAVLLM SEAEADRRGL QPLGRIASWA TAGVDPQIMG TGPIPASRKA LSKAGWAVSD LDLVEANEAF AAQSCTVVRE LGLDPDIVNV NGGAIAIGHP IGASGARVLN TLLFEMKRRS AKKGLVTLCI GGGMGVAMCI EGM //