ID T0K479_9SPHN Unreviewed; 402 AA.
AC T0K479;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN ORFNames=M529_15090 {ECO:0000313|EMBL:EQB31359.1};
OS Sphingobium ummariense RL-3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB31359.1, ECO:0000313|Proteomes:UP000015523};
RN [1] {ECO:0000313|EMBL:EQB31359.1, ECO:0000313|Proteomes:UP000015523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB31359.1,
RC ECO:0000313|Proteomes:UP000015523};
RX PubMed=24233594;
RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT Hexachlorocyclohexane-Degrading Bacterium.";
RL Genome Announc. 1:e00956-13(2013).
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:EQB31359.1}.
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DR EMBL; AUWY01000102; EQB31359.1; -; Genomic_DNA.
DR RefSeq; WP_021318763.1; NZ_AUWY01000102.1.
DR AlphaFoldDB; T0K479; -.
DR STRING; 1346791.M529_15090; -.
DR PATRIC; fig|1346791.3.peg.2904; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 7181944at2; -.
DR Proteomes; UP000015523; 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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000015523};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EQB31359.1}.
FT DOMAIN 5..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..401
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 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 402 AA; 41871 MW; 794C0409B82D8145 CRC64;
MSDAFICDAI RTPIGRFGGA LSTVRADDLA AIPIRALIER NPGVNWQAVD DVLLGCANQA
GEDNRNVARM ATLLAGLPKE VSGSTVNRLC GSGLDAVGSA ARAIRAGDAE LIIAGGVESM
SRAPYVMGKA DTAFSRGQRL EDTTIGWRFV NPAMKAAYGV DTMPETGENV AQEWGVSRED
QDAFALASQR KAVAAQANGR LACEIVSVII PQKKGDPITV AQDEHPRPNT TLEGLAKLRP
IVRPDGTVTA GNASGVNDGA AAMVVASEEA AKRHGLKPRA RVVAMAAAGV APRVMGIGPV
NAARKLLALG GGLSIDQLDV IELNEAFASQ AIAVLRDLGL QPDDERVNRN GGAIALGHPL
GMSGARIAMS AVEELDRSRG RYAMVFMCVG VGQGIGLLLE RI
//
