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Database: UniProt
Entry: A0A0T1SI76_9ACTN
LinkDB: A0A0T1SI76_9ACTN
Original site: A0A0T1SI76_9ACTN 
ID   A0A0T1SI76_9ACTN        Unreviewed;       385 AA.
AC   A0A0T1SI76;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQX53433.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:KQX53433.1};
GN   ORFNames=ASD33_09685 {ECO:0000313|EMBL:KQX53433.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX53433.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX53433.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX53433.1,
RC   ECO:0000313|Proteomes:UP000051136};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQX53433.1}.
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DR   EMBL; LMEP01000012; KQX53433.1; -; Genomic_DNA.
DR   RefSeq; WP_056560797.1; NZ_LMEP01000012.1.
DR   AlphaFoldDB; A0A0T1SI76; -.
DR   STRING; 1736450.ASD33_09685; -.
DR   Proteomes; UP000051136; Unassembled WGS sequence.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:KQX53433.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051136};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQX53433.1}.
FT   DOMAIN          5..254
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          263..384
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        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        371
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   385 AA;  40592 MW;  147FC1872796AC05 CRC64;
     MAEAYIVEAV RTPVGRRKGG LASVHPADLG AHVLKALVAR SGIDPAAVED VVFGCLDTVG
     PQAGDIARTA WLAAGLPEEV PGVTVDRQCG SSQQAVHFAA QGVLSGTQDL VVAGGTQNMS
     MIPIAFASRQ AAEPLGFTEG PYAGSEGWRA RYGDAPVNQF HGAELIAKKW GITRRDQEEF
     ALRSHERALR AIDEGRFARE TVAYGEVTAD EGPRRDTTLE KMAGLKTVVE GGTITAACSS
     QVSDGAAAML LASERAVREH GLTPRARIHH LSVRGEDPIR MLSAPIPATA YALKKIGLTI
     DDMDLVEINE AFAPVVLAWL KETGADPARV NVNGGAIALG HPLGATGVKL MTTLLHELER
     TGGRYGLQTM CEGGGQANVT IIERL
//
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