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
//