ID A0A1P8Y0Y9_9ACTN Unreviewed; 392 AA.
AC A0A1P8Y0Y9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=BV401_30545 {ECO:0000313|EMBL:AQA14106.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA14106.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
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; CP019458; AQA14106.1; -; Genomic_DNA.
DR RefSeq; WP_069866784.1; NZ_CP019458.1.
DR AlphaFoldDB; A0A1P8Y0Y9; -.
DR STRING; 75293.BV401_30545; -.
DR KEGG; sauo:BV401_30545; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000187851; 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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AQA14106.1}.
FT DOMAIN 2..258
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 267..387
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 84
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 40328 MW; 6720A50FA793CD96 CRC64;
MMVAGARTPM GRLLGSLRSF SGADLGGIAI KAALERAGVG ADQVQYVIMG QVLQAGTGQI
PARQAAVKAG IPMSVPALTI NKVCLSGLDA IALADQLIRA GEFDIVVAGG QESMTNAPHL
LPKSREGYKY GAVEMIDAMA HDGLTDAFES IAMGESTEKH NTRLGIQRPE QDEFAAQSHQ
RAAAAQKNGL FDAEITPVEI PQRKGEPVVF DKDEGIRGET TAELLARLKP AFTKDGTITA
GTSSQISDGA AAVVVMSKAK AEELGLEWIA EIGAHGNVAG PDNSLQSQPS NAIAHALGKE
GLTVDDLDLI EINEAFAAVA VQSMKDLGVS PEKVNVNGGA IALGHPIGMS GARIALHLAL
ELRRRGGGTG AAALCGGGGQ GDALILRVPA GE
//
