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Database: UniProt
Entry: A0A345XN46_9ACTN
LinkDB: A0A345XN46_9ACTN
Original site: A0A345XN46_9ACTN 
ID   A0A345XN46_9ACTN        Unreviewed;       434 AA.
AC   A0A345XN46;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:AXK33062.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:AXK33062.1};
GN   ORFNames=DVA86_10785 {ECO:0000313|EMBL:AXK33062.1};
OS   Streptomyces armeniacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK33062.1, ECO:0000313|Proteomes:UP000254425};
RN   [1] {ECO:0000313|EMBL:AXK33062.1, ECO:0000313|Proteomes:UP000254425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK33062.1,
RC   ECO:0000313|Proteomes:UP000254425};
RA   Labana P., Gosse J.T., Boddy C.N.;
RT   "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; CP031320; AXK33062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345XN46; -.
DR   Proteomes; UP000254425; 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; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR   PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:AXK33062.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254425};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AXK33062.1}.
FT   DOMAIN          15..288
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          297..433
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        100
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        420
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   434 AA;  45875 MW;  CDE90693FDBF6F8C CRC64;
     MSSSGLIRSQ VPRRVAVIGG SRIPFARADG PYATCSNQDL LTAALGGLVE RHGLHGERAI
     GEVVAGAVLK HSRDFNLARE SVLSTGLDPR TPAYDIQQAC ATSLQAVIAV ANKIALGQID
     SGIAGGADTT SDPPIAMNDR LRRILLATRR AKTLRARTRE IAPVRPKHLL PEIPRNAEPC
     TGRSMGEHAA QTAKEWGITR LEQDELAARS HRNLATAYDS GFLHDLVVPF NGLARDQNLR
     PGTSVQKLGE LEPVFGVTEG EVTGEATMTP GNSTPLSDGA ATVLLAGEEW ARERGLRPLA
     YLTAYETGAV DFTEDAGEGL LMAPAFAVPR MLRRVGLGME DFELVEIHEA FASQVLATMA
     AWEKQGLAPV DRSRLNTAGS SLATGHPFAA TGARIVATLA KLLAEREGAR PGARGLISIC
     AAGGQGVTAI LERA
//
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