ID A0A0T1QHH0_9ACTN Unreviewed; 389 AA.
AC A0A0T1QHH0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQX16786.1};
GN ORFNames=ASC82_00565 {ECO:0000313|EMBL:KQX16786.1};
OS Streptomyces sp. Root431.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736535 {ECO:0000313|EMBL:KQX16786.1, ECO:0000313|Proteomes:UP000051818};
RN [1] {ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|Proteomes:UP000051818};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX16786.1, ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|EMBL:KQX16786.1,
RC ECO:0000313|Proteomes:UP000051818};
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:KQX16786.1}.
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DR EMBL; LMEI01000001; KQX16786.1; -; Genomic_DNA.
DR RefSeq; WP_056639836.1; NZ_LMEI01000001.1.
DR AlphaFoldDB; A0A0T1QHH0; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000051818; Unassembled WGS sequence.
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; 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; 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.
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:KQX16786.1}.
FT DOMAIN 6..257
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 266..388
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
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 389 AA; 41397 MW; 4502C92191C01592 CRC64;
MAAEPVIVEA VRTPIGKRGG ALANLHPAYL LGETYRELLG RTGIHADCVE QIVGGTVTHA
GEQSMNPART AWLTMGLPYE TAATTVDCQC GSSQQASHMV ANMVAAGAID IGISCGVEAM
SRVPLGSGSK HGPGKPFPDE WNVDLPNQFE AAERIARRRG LTRERVDSLG LLSQERAAVA
WAEERYKRET FAVQVPTTEA EQAAGQGMWR LVDRDEGLRD TSMEGLARLK PVMPTAVHTA
GNSSQISDGA SAIMWASKRM ARALKLKPRA RIVAQALVGA DPHFHLDGPI DATRAVLGKA
GMSLKDIDLV EINEAFASVV LSWAQVFDQD LEKVNVNGGA IAIGHPVGAT GARLITTALH
ELERTDKEFA LITMCAGGAL ATGTIIQRL
//
