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Database: UniProt
Entry: A0A1G6PNJ0_9BURK
LinkDB: A0A1G6PNJ0_9BURK
Original site: A0A1G6PNJ0_9BURK 
ID   A0A1G6PNJ0_9BURK        Unreviewed;       400 AA.
AC   A0A1G6PNJ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=SAMN05192589_103294 {ECO:0000313|EMBL:SDC81753.1};
OS   Paracidovorax valerianellae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=187868 {ECO:0000313|EMBL:SDC81753.1, ECO:0000313|Proteomes:UP000198781};
RN   [1] {ECO:0000313|EMBL:SDC81753.1, ECO:0000313|Proteomes:UP000198781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16619 {ECO:0000313|EMBL:SDC81753.1,
RC   ECO:0000313|Proteomes:UP000198781};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FMZC01000003; SDC81753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6PNJ0; -.
DR   STRING; 187868.SAMN05192589_103294; -.
DR   OrthoDB; 8558405at2; -.
DR   Proteomes; UP000198781; 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; 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:UP000198781};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SDC81753.1}.
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;  41560 MW;  D88A6230E57B12ED CRC64;
     MTQAFICDAI RTPFGRYGGA LSSVRTDDLG AIPLKALMAR NPGVDWAAVT DVLYGCANQA
     GEDNRNVARM AALLAGLPID VPGATINRLC GSGLDAVGTA ARAIKAGEAG LMIAGGVESM
     SRAPFVMPKA ETAFSRTNAV YDTTIGWRFV NKLMKAQYGV DSMPETAENV ADDYRIEREA
     QDRMALASQL KAVAAQQAGH LAREITPVHV PQKKGDPVVV DKDEHPRETS LEALARLKPV
     VREGGTVTAG NASGVNDGAC ALLLADEASA AKHGLTPKAR VVGMATAGVA PRVMGIGPAP
     ATQKVLQLTG LTLEQMDVIE LNEAFAAQGI AVLRQLGLQD DDERVNAWGG AIALGHPLGA
     SGARLATTAV NRLHATGGRY ALATMCIGVG QGIAVVLERV
//
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