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Database: UniProt
Entry: A0A1P8YG51_9NOCA
LinkDB: A0A1P8YG51_9NOCA
Original site: A0A1P8YG51_9NOCA 
ID   A0A1P8YG51_9NOCA        Unreviewed;       383 AA.
AC   A0A1P8YG51;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase family protein {ECO:0000313|EMBL:AQA23094.1};
GN   ORFNames=BTZ20_0634 {ECO:0000313|EMBL:AQA23094.1};
OS   Rhodococcus sp. MTM3W5.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA23094.1, ECO:0000313|Proteomes:UP000187995};
RN   [1] {ECO:0000313|EMBL:AQA23094.1, ECO:0000313|Proteomes:UP000187995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA23094.1,
RC   ECO:0000313|Proteomes:UP000187995};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; CP019572; AQA23094.1; -; Genomic_DNA.
DR   RefSeq; WP_077040304.1; NZ_CP019572.1.
DR   AlphaFoldDB; A0A1P8YG51; -.
DR   STRING; 1805827.BTZ20_0634; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000187995; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR   PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AQA23094.1}.
FT   DOMAIN          5..251
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          261..381
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        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        368
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   383 AA;  40028 MW;  6F0EDD686B165102 CRC64;
     MAEAYIVDAV RTAVGRKNGA LSAVHPIDLG ASVIRSLTDR NPIDPAAIDD VMFGCVDTIG
     GQAGNIARTS ALAAGLPEGV PGVTVDRQCG SSQQALHFAA QAVLSGTADL IVAGGVQSMS
     RIPISAAMTA GREFGFDDPY SGSEDWRRRY GNTEISQFRA AELIAEKWGI SRLEMEQWAL
     RSHQRARDAI AGGRFDGEIV PVGSFEVDEC PRDTSLAKMA ALPPLREGGR LTAALASQIS
     DGASAVLVAS AAALKTHNLV PRARIHHLSA RGADPVFMLT APIPATEYAL GKTGMSIDDF
     DVIEINEAFA SVVLAWLAET GADPERVNVN GGGIALGHPL GATGTKLFGT LLNELERTGG
     RYGLQTMCEG GGTANVLIVE RLG
//
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