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Database: UniProt
Entry: A0A1C4NN72_9ACTN
LinkDB: A0A1C4NN72_9ACTN
Original site: A0A1C4NN72_9ACTN 
ID   A0A1C4NN72_9ACTN        Unreviewed;       406 AA.
AC   A0A1C4NN72;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acetyl-CoA acyltransferase {ECO:0000313|EMBL:SCD99633.1};
GN   ORFNames=GA0115234_1055338 {ECO:0000313|EMBL:SCD99633.1};
OS   Streptomyces sp. DvalAA-43.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCD99633.1, ECO:0000313|Proteomes:UP000199186};
RN   [1] {ECO:0000313|EMBL:SCD99633.1, ECO:0000313|Proteomes:UP000199186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCD99633.1,
RC   ECO:0000313|Proteomes:UP000199186};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; FMBW01000043; SCD99633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4NN72; -.
DR   OrthoDB; 3204099at2; -.
DR   Proteomes; UP000199186; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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   ECO:0000313|EMBL:SCD99633.1};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SCD99633.1}.
FT   DOMAIN          8..266
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          276..397
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        96
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        385
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   406 AA;  43177 MW;  405138FE91CBBEB3 CRC64;
     MPRTIRDVVF VDGVRTPFGK AGPKGIYHET RADDLVVKAI RELLRRNPDL DPARIDEVAI
     AATTQIGDQG LTLGRTAGIL AGLPQSVPGY SIDRMCAGAL TAVTSTAGSI AFGAYDVVVA
     GGVEHMGRHP MGEGVDPNPR FVSEKLVDES ALFMGMTAEN LHDRYPQITK VRADEYAVRS
     QEKAAKAYAN GKIQQDLVPI SVRRTNAEAG ETGWGLVTAD EPMRPGTTME SLAGLKTPFR
     AHGRVTAGNA AGLNDGATAS LLAAEDVARE LGLPVRMRLV SYAFAGVEPE VMGYGPIPAT
     EKALAKAGLT IDDIGLFEIN EAFAVQVLAF LDHYGIADDD ARVNQYGGAI AYGHPLASSG
     VRLMTQLARQ FEEQPEVRYG VTTMCVGFGM GATVIWENPN FDGGSK
//
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