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Database: UniProt
Entry: A0A161R3E9_9BRAD
LinkDB: A0A161R3E9_9BRAD
Original site: A0A161R3E9_9BRAD 
ID   A0A161R3E9_9BRAD        Unreviewed;       417 AA.
AC   A0A161R3E9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KZD23471.1};
GN   ORFNames=A4A58_27560 {ECO:0000313|EMBL:KZD23471.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD23471.1, ECO:0000313|Proteomes:UP000076574};
RN   [1] {ECO:0000313|EMBL:KZD23471.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD23471.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT   Fed.";
RL   Submitted (MAR-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:KZD23471.1}.
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DR   EMBL; LVYV01000011; KZD23471.1; -; Genomic_DNA.
DR   RefSeq; WP_068732667.1; NZ_LVYV01000011.1.
DR   AlphaFoldDB; A0A161R3E9; -.
DR   STRING; 943830.A4A58_27560; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000076574; 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   Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KZD23471.1}.
FT   DOMAIN          5..235
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          295..416
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        403
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   417 AA;  43910 MW;  4AFC341827EE883B CRC64;
     MADAYIIDAV RTPRGIGKVG KGKLAEQHPQ HLAATVLKAI AERNKLNTAD VDDVIWSTST
     QRGKQGGDLG RMAALDAGYD IKASGTTLDR FCGGGITAVN FAAAQIMSGM EDVVIAGGTE
     MMSLTGAMAA EDMAAGKPPL GMGSGNKRLA KVHPQSHQGI CGDAIASMEG ISREALDALG
     LESQRRAAIA IKEGRFDKSI VPVKDDEGNI VLAKDEYPRP ETTAEGLAGL KPAFAAMADH
     PLDESGMTFR KQINQKYPDL KIEHFHHAGN SSGVVDGAAA LLLTSKSYAD KHGLKLRARI
     VAMANIGDDP TLMLNAPVPA AKKVLAKAGL KKEDIDLWEI NEAFAVVAEK FIRDLDLDRS
     KVNVNGGSIA LGHPIGATGA ILIGTVLDEL ERRNLKRGLV TMCAAGGMAP AIIIERV
//
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