ID F7QGT7_9BRAD Unreviewed; 402 AA.
AC F7QGT7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN ORFNames=CSIRO_0701 {ECO:0000313|EMBL:EGP09543.1};
OS Bradyrhizobiaceae bacterium SG-6C.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP09543.1, ECO:0000313|Proteomes:UP000003148};
RN [1] {ECO:0000313|EMBL:EGP09543.1, ECO:0000313|Proteomes:UP000003148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP09543.1,
RC ECO:0000313|Proteomes:UP000003148};
RX PubMed=21742875; DOI=10.1128/JB.05647-11;
RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA Pandey G.;
RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT Bradyrhizobiaceae Strain SG-6C.";
RL J. Bacteriol. 193:5057-5057(2011).
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:EGP09543.1}.
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DR EMBL; AFOF01000011; EGP09543.1; -; Genomic_DNA.
DR AlphaFoldDB; F7QGT7; -.
DR STRING; 709797.CSIRO_0701; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_5; -.
DR Proteomes; UP000003148; 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 ECO:0000313|EMBL:EGP09543.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EGP09543.1}.
FT DOMAIN 4..269
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; 42029 MW; 8469C3D29F808C52 CRC64;
MRDVYICDAV RTPIGRFGGS LAKVRADDLA AAPIKALMER NAKADWGALD EVSYGCANQA
GEDNRNVARM ALLLAGLPEN VPGMTVNRLC ASGLDAVGGI ARAIRAGEID FAIAGGVESM
TRAPFVTGKA NEAYQRAVET YDTTIGWRFV NPLMKKMYGV DSMPETGENV ATDYQISRED
QDAFAIRSQQ RAGKAIAAGY FAEEIVPVTV AGGKAGPVIV DKDEHPRPET TLEQLAKLKP
VTRPDGTVTA GNASGVNDGA AAIILASEEA VKKHGLTPRA KLLAHASAGV APRVMGMGPV
PAVRKLLEKL GLKISDIDLI ELNEAFASQG LAVLRQLGVK EDSDFVNPHG GAIALGHPLG
MSGARLVLTA VHGLEKRGGK YALATMCVGV GQGAAAAIEK VN
//