ID   H1SBZ9_9BURK            Unreviewed;       400 AA.
AC   H1SBZ9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=OR16_28614 {ECO:0000313|EMBL:EHP39978.1};
OS   Cupriavidus basilensis OR16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP39978.1, ECO:0000313|Proteomes:UP000005808};
RN   [1] {ECO:0000313|EMBL:EHP39978.1, ECO:0000313|Proteomes:UP000005808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR16 {ECO:0000313|EMBL:EHP39978.1,
RC   ECO:0000313|Proteomes:UP000005808};
RX   PubMed=22461549; DOI=10.1128/JB.06752-11;
RA   Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA   Nagy I., Horvath B., Nagy I., Kukolya J.;
RT   "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL   J. Bacteriol. 194:2109-2110(2012).
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}.
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:EHP39978.1}.
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DR   EMBL; AHJE01000077; EHP39978.1; -; Genomic_DNA.
DR   RefSeq; WP_006161349.1; NZ_AHJE01000077.1.
DR   AlphaFoldDB; H1SBZ9; -.
DR   PATRIC; fig|1127483.3.peg.5712; -.
DR   OrthoDB; 8951704at2; -.
DR   Proteomes; UP000005808; Unassembled WGS sequence.
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; 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; 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}.
FT   DOMAIN          5..267
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          275..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;  41616 MW;  C8BD828CFBC57133 CRC64;
     MTEAFICDAI RTPIGRYGGS LSGVRPDDLG AVPLKALMAR NPNLDWSAID DVIYGNANQA
     GEDNRNVARM SLLLAGLPQS VPGATINRLC GSGMDATGTA ARAIKSGEAG LMLAGGVESM
     SRAPFVMGKA TSAFSRDAQI FDTTIGWRFI NPAMRAAYGV DSMPETAENV ATDYKISRED
     QDLMALRSQE KASRAQADGT LAQEIAAVTI AQKKGDPLVV ERDEHPRATS MEALGKLRGV
     VRADGTVTAG NASGVNDGAC AILLASEAAA RQHGLTPKAR IVGMATAGVA PRVMGIGPAP
     ASQKLLKQLG MTIDQMDVIE LNEAFAAQGL AVLRELGVAD DDARVNPNGG AIALGHPLGM
     SGARLVTTAM YQLHRTGGRF ALCTMCIGVG QGIAMVIERV
//