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Database: UniProt
Entry: F7QGT7_9BRAD
LinkDB: F7QGT7_9BRAD
Original site: F7QGT7_9BRAD 
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
//
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