ID H5YKT0_9BRAD Unreviewed; 402 AA.
AC H5YKT0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN ORFNames=Bra471DRAFT_07362 {ECO:0000313|EMBL:EHR06507.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR06507.1};
RN [1] {ECO:0000313|EMBL:EHR06507.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR06507.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-2011) 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; CM001442; EHR06507.1; -; Genomic_DNA.
DR RefSeq; WP_007615978.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YKT0; -.
DR HOGENOM; CLU_031026_2_2_5; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000005774; Chromosome.
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 Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 4..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..400
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 402 AA; 41856 MW; 39853E6ACDF059D1 CRC64;
MRDVFICDAV RTPIGRFGGS LAKVRADDLA AAPIKALMAK HPNLEWAEVD EVFFGCANQA
GEDNRNVARM ALLLAGLPDS VPGQTLNRLC ASGLDAVGAA GRAIRSGEIE LAIAGGVESM
TRAPFVMGKA QEAFSRSAEI FDTTIGWRFI NPLLKAQYGV DAMPETGENV AEEFQVSRAD
QDAFAIRSQQ RAGAAIAAGY FAEEITPITI PGGKAGPVIV DKDEHPRPET TLEALTKLRP
IVRNPGTVTA GNASGVNDGA AAMILASEAA VKKHGLTPRA RILGLASAGV PPRIMGIGPV
PATRKLMARL GKKISDFDLI ELNEAFASQG IACMRQLGVA DDADFVNPHG GAIALGHPLG
MSGARLALTA VHGMEKRGGK LALATMCVGV GQGVAVAIEK LN
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