ID A0A0A1VKL6_9BURK Unreviewed; 400 AA.
AC A0A0A1VKL6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN ORFNames=AVS7_03449 {ECO:0000313|EMBL:GAD23689.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD23689.1};
RN [1] {ECO:0000313|EMBL:GAD23689.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD23689.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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; DF238950; GAD23689.1; -; Genomic_DNA.
DR RefSeq; WP_020230762.1; NZ_DF238950.1.
DR AlphaFoldDB; A0A0A1VKL6; -.
DR STRING; 1268622.AVS7_03449; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 8558405at2; -.
DR Proteomes; UP000030646; 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:UP000030646};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..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; 41432 MW; 0C2EFC7A41C21F7D CRC64;
MTQAFICDAV RTPFGRYGGA LAGVRADDLG AVPIRALMQR NSGVDWAAVT DVLYGCANQA
GEDNRNVARM SALLAGLPID VPGATINRLC GSGLDAVGSA ARTIKAGEAG LMIAGGVESM
SRAPFVMPKA ESAFSRSNAV YDTTIGWRFV NRLMKAQYGV DSMPETAENV ADDFRIEREA
QDRMALASQQ KAAAAIAAGH LAQEIVPVTI AQKKGDPIVV SQDEHPRATT LEALAKLKGV
VREGGTVTAG NASGVNDGAC ALLLASEEAA RQYGLTPRAR VVGMATAGVA PRIMGFGPAP
AVRKVLALTG LTLDQMDVIE LNEAFAAQGL AVLRDLGIAD DDKRVNQWGG AIALGHPLGA
SGARLATTAV SQLHTLGGRY ALCTMCIGVG QGIAVILERV
//
