ID A0A0K1K1T8_9BURK Unreviewed; 392 AA.
AC A0A0K1K1T8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AKU23146.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:AKU23146.1};
GN ORFNames=ACZ75_18495 {ECO:0000313|EMBL:AKU23146.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU23146.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU23146.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU23146.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-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}.
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DR EMBL; CP012201; AKU23146.1; -; Genomic_DNA.
DR RefSeq; WP_050410240.1; NZ_CP012201.1.
DR AlphaFoldDB; A0A0K1K1T8; -.
DR STRING; 1678028.ACZ75_18495; -.
DR KEGG; mnr:ACZ75_18495; -.
DR PATRIC; fig|1678028.3.peg.3757; -.
DR OrthoDB; 8558405at2; -.
DR Proteomes; UP000056897; Chromosome.
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; 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:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 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; 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:AKU23146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000056897};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 4..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..391
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 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 392 AA; 40515 MW; 04726B084B4764A6 CRC64;
MDDVVIVAAG RTAVGKFGGS LAKIPASELG AHVIKGLLAQ TGIDPNLISE AILGQVLTAA
VGQNPARQAV IKAGLPSAIP AYTINKVCGS GLKATHLAAQ AIKCGDANII IAGGQENMSA
APHALNGSRD GFRMGDAKMV DTMIVDGLWD VYNQYHMGVT AENVAKKYEI SRAEQDEFAL
ASQQKAEAAQ KAGKFKDEIL PLEIVQKKGS IVFDSDEYIK AGSTLDALSS LRPAFSKEGS
VTAGNASGIN DGAAAVIMMT ATQAKQLGLK PLARIKSYAS SGLDPAVMGL GPVSASKLCL
QKAGWTPQDL DLMEINEAFA AQAIAVNREM GWDTSKINVN GGAIAIGHPI GASGARILVT
LLHEMARRDA KKGLASLCIG GGMGVALAVE RD
//