ID   I3TS97_TISMK            Unreviewed;       410 AA.
AC   I3TS97;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Acetyl-CoA acyltransferase {ECO:0000313|EMBL:AFK55635.1};
GN   OrderedLocusNames=TMO_a0232 {ECO:0000313|EMBL:AFK55635.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM1 {ECO:0000313|EMBL:AFK55635.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55635.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55635.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM1 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; CP003237; AFK55635.1; -; Genomic_DNA.
DR   RefSeq; WP_014747312.1; NC_017957.2.
DR   AlphaFoldDB; I3TS97; -.
DR   KEGG; tmo:TMO_a0232; -.
DR   PATRIC; fig|1110502.3.peg.3886; -.
DR   HOGENOM; CLU_035425_4_0_5; -.
DR   Proteomes; UP000005258; Plasmid pTM1.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00829; SCP-x_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   PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 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:AFK55635.1}; Plasmid {ECO:0000313|EMBL:AFK55635.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AFK55635.1}.
FT   DOMAIN          5..207
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          283..377
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   410 AA;  43001 MW;  A21B0F7DC411CBBA CRC64;
     MEKTYIVGIG MSHFGRFLNR GLADLTGEAV TEALADSGLA AHDIGAAYFA NASQGVVEGQ
     HLVRGQLALR RLGFQNLSIT NVENACASGS TALNAAVAYI ASGQGDVALA VGADKMNAPD
     RALSFAIFDG AWDVGDVEGQ IARLERLGQA MQPPERAVEP GQRSVFMDVY AALARFHMGT
     FGTTQADIAQ VAAKNHSHSV LNPKAQYRHA MTADEVLAAR EISWPLTLPM CAPISDGAAA
     AIVVSEKKAR RMGLTRAVRI AASVQAAGSD RAAEDLDRHI CRRAVDRAYE LSGIGPEDVS
     VVEVHDATAF AELQQAELLR LCPMGEGGRL ATSGATTLGG RIPINVSGGL ESRGHPIGAT
     GLAQIYELVT QLRGEAGPRQ VEGARVGLAE NGGGFHGYEE AVAVITLLQR
//