ID A0A1A0UA52_9MYCO Unreviewed; 393 AA.
AC A0A1A0UA52;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=A5758_10970 {ECO:0000313|EMBL:OBB67901.1};
OS Mycobacterium sp. 852014-50255_SCH5639931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB67901.1, ECO:0000313|Proteomes:UP000092113};
RN [1] {ECO:0000313|EMBL:OBB67901.1, ECO:0000313|Proteomes:UP000092113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB67901.1,
RC ECO:0000313|Proteomes:UP000092113};
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}.
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:OBB67901.1}.
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DR EMBL; LZSV01000016; OBB67901.1; -; Genomic_DNA.
DR RefSeq; WP_067739031.1; NZ_LZSV01000016.1.
DR AlphaFoldDB; A0A1A0UA52; -.
DR STRING; 1834112.A5758_10970; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000092113; 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; IPR020615; Thiolase_acyl_enz_int_AS.
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; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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; PS00098; THIOLASE_1; 1.
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:OBB67901.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..391
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40619 MW; E01D1DF32872CF7C CRC64;
MTTSVIVAGA RTPIGKLMGS LKDFSASDLG GIAIAGALEK ANVPASAVEY VIMGQVLTAG
AGQMPARQAA VAAGIGWDVP ALTINKMCLS GIDAIALADQ LIRAGEFDVV VAGGQESMTK
APHLLMDSRA GYKYGDVTVL DHMAYDGLYD VFTDQPMGAL TEQRNDVDKF TRQEQDEFAA
RSHQKAAAAW KDGVFADEVV PVNIPQRKGD SLQFTEDEGI RANTTAESLA GLKPAFRRDG
TITAGSASQI SDGAAAVVVM NKAKAQELGL TWLVEIGAHG VVAGPDSTLQ SQPANAIKKA
LSREGISVDQ LDVVEINEAF SAVALASTRE LGLDPEIVNV NGGAIAVGHP IGMSGARITL
HAALELARRG SGYAVAALCG AGGQGDALIL RAK
//
