ID D7CDB4_STRBB Unreviewed; 382 AA.
AC D7CDB4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ADI12956.1};
GN OrderedLocusNames=SBI_09838 {ECO:0000313|EMBL:ADI12956.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI12956.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI12956.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI12956.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI12956.1; -; Genomic_DNA.
DR RefSeq; WP_014182403.1; NC_016582.1.
DR AlphaFoldDB; D7CDB4; -.
DR STRING; 749414.SBI_09838; -.
DR KEGG; sbh:SBI_09838; -.
DR PATRIC; fig|749414.3.peg.10131; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_11; -.
DR Proteomes; UP000000377; 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; -; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ADI12956.1}.
FT DOMAIN 5..252
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 259..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 382 AA; 39608 MW; 53508C1CE90F0CAC CRC64;
MSEAFIVGAV RTPVGRRKGA LSGVHPADLG AHVLRALLER TGADPGAVDD VYFGCVSQIG
AQTGNIARTA WLSAGLPQHV PGTTIDRQCG SSQQAVHFAA QAVGSGTADL VVAGGVETMS
LVPIAAPMTV GEQAGMGSPY AGSGWRERYG DQEVSQFRGA ELIAEKWGIS RADMEEFALT
SHQRALAAQA DGAFDDEITP AFGLTADEGP RADTTLEKMA GLKTLTEDGR LTAAVSSQIS
DGAAALLIAS EEAVRRHGLT PLARVHTMAV VGSDPIHMLT GPIPATERVL EKAGLSIDDI
DLIEINEAFA SVVLAWQKEI GAPLDRVNAF GGAIALGHPL GATGARLMTT LVHQLRSTGG
RHGLQTMCEG GGMANAIVLE RL
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