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Database: UniProt
Entry: A0A2N0FQP2_9FLAO
LinkDB: A0A2N0FQP2_9FLAO
Original site: A0A2N0FQP2_9FLAO 
ID   A0A2N0FQP2_9FLAO        Unreviewed;       404 AA.
AC   A0A2N0FQP2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=B0O79_0376 {ECO:0000313|EMBL:PKA96737.1};
OS   Flavobacteriaceae bacterium MAR_2009_75.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250285 {ECO:0000313|EMBL:PKA96737.1, ECO:0000313|Proteomes:UP000232536};
RN   [1] {ECO:0000313|EMBL:PKA96737.1, ECO:0000313|Proteomes:UP000232536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2009_75 {ECO:0000313|EMBL:PKA96737.1,
RC   ECO:0000313|Proteomes:UP000232536};
RA   Teeling H.;
RT   "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT   Genomic & Taxonomic Observatory).";
RL   Submitted (NOV-2017) 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}.
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:PKA96737.1}.
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DR   EMBL; PHTZ01000001; PKA96737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0FQP2; -.
DR   OrthoDB; 9764892at2; -.
DR   Proteomes; UP000232536; 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:SF11; 3-KETOACYL-COA THIOLASE FADA; 1.
DR   PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          5..269
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        357
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        387
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   404 AA;  43135 MW;  8ED672D659DA024C CRC64;
     MKEAYIVDAT RTPIGSFRGA LAQVRADDLA AIPIKALLEK YPNLPKDAID DVILGCHNQA
     GEDNRNVARM ALLLAGLPYT VPGETINRLC SSGMSAVVQA NRAIKAGDGD VFIAGGMEHM
     SRGPLVISKS AIAFGNDSQM EDSSFGWRFV NKKLHEMYGT DAMGITAENL AEMFSISRED
     QDLFAYNSQM KAAKAQQNGI LGEEICPVEI PQRKGDPIIV SQDEFIRPST TIEKLATLRT
     VFKKDGTVTA GNASGLNDGA AAMLVVSEDA LKKYYLTPKA RIVASAVVGV EPKIMGIGPV
     YATRKVLAKA GLELKDMDVL EFNEAFSAQA LACTRELGLK DDDPRINPNG GAIAIGHPLG
     MSGTRILQAA TNELVRSGGK YGLATMCVGV GMGYATIIEN VNQY
//
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