ID   A0A160FNG0_9BURK        Unreviewed;       400 AA.
AC   A0A160FNG0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=AYM40_18235 {ECO:0000313|EMBL:ANB74092.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB74092.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB74092.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB74092.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA;
CC         Xref=Rhea:RHEA:19481, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.3.1.174;
CC         Evidence={ECO:0000256|ARBA:ARBA00000708};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000256|ARBA:ARBA00005211}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; CP014578; ANB74092.1; -; Genomic_DNA.
DR   RefSeq; WP_063497442.1; NZ_CP014578.1.
DR   AlphaFoldDB; A0A160FNG0; -.
DR   STRING; 1804984.AYM40_18235; -.
DR   KEGG; buz:AYM40_18235; -.
DR   Proteomes; UP000076852; Chromosome 1.
DR   GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR012793; PcaF.
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   NCBIfam; TIGR02430; pcaF; 1.
DR   PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          5..267
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          277..399
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        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   400 AA;  42275 MW;  4945AB0C20C98496 CRC64;
     MNDAFICDAI RTPIGRYGGA LKDVRADDLG AVPIKALIER NPGVDWRAID DVIYGCANQA
     GEDNRNVARM SALLAGLPTD TPGATINRLC GSGMDAVGTA ARAIKAGEAR LMIAGGVESM
     TRAPFVMGKA TSAFSRQADI YDTTIGWRFI NPLMKRQYGV DSMPETAENV AVEFSVSRAD
     QDAFALSSQQ KAARAQRDGT LAQEIVGVEI AQKKGDPVRV TLDEHPRETT LESLGKLKGV
     VRPDGSVTAG NASGVNDGAC ALLLANQAAA DQYGLRRRAR VAGMATAGVE PRIMGIGPAP
     ATQKLLKQLN MTFEQFDVIE LNEAFASQGL AVLRTLGLRD DDPRVNPNGG AIALGHPLGA
     SGARLITTAL YQLERINGRF ALCTMCIGVG QGIALVIERL
//