ID D3PRK2_MEIRD Unreviewed; 402 AA.
AC D3PRK2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN OrderedLocusNames=Mrub_1323 {ECO:0000313|EMBL:ADD28085.1};
GN ORFNames=K649_06270 {ECO:0000313|EMBL:AGK04554.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04554.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:ADD28085.1, ECO:0000313|Proteomes:UP000006655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC {ECO:0000313|EMBL:ADD28085.1};
RX PubMed=21304689; DOI=10.4056/sigs.1032748;
RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Meiothermus ruber type strain (21).";
RL Stand. Genomic Sci. 3:26-36(2010).
RN [2] {ECO:0000313|EMBL:AGK04554.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK04554.1};
RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA Eichler E., Turner S.W.;
RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT Sequencing Data.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGK04554.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC {ECO:0000313|EMBL:AGK04554.1};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) 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; CP001743; ADD28085.1; -; Genomic_DNA.
DR EMBL; CP005385; AGK04554.1; -; Genomic_DNA.
DR RefSeq; WP_013013604.1; NC_021081.1.
DR AlphaFoldDB; D3PRK2; -.
DR STRING; 504728.K649_06270; -.
DR KEGG; mrb:Mrub_1323; -.
DR KEGG; mre:K649_06270; -.
DR PATRIC; fig|504728.9.peg.1291; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 23995at2; -.
DR Proteomes; UP000006655; Chromosome.
DR Proteomes; UP000013026; 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:ADD28085.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AGK04554.1}.
FT DOMAIN 6..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..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; 42359 MW; 69DDF0FDF789D82A CRC64;
MTMEAYILDA VRTPVGKHGG ALSSVRPDDL GAIPLKALLE RTGIPGSDVE DVYMGCANQA
GEDNRNVARM SLLLAGLPIS VGGSTVNRLC GSGLDAVASA ARAIWAGEGQ VYLGGGVESM
SRAPWVMPKA EKGFATGNVT LYDTTLGWRL VNPRMKELYG TEAMGETAEN LAEQYKISRE
AQDRFALHSH QKAIRAQQSG AYASQMVPVE VKDRKGNTTL VQTDEGPRAD TSLEALAQLR
PVFRAGGSVT AGNSSSLNDG AAAVLLVADA YARAHGLKPM ARVRAIAVAG VEPRIMGIGP
VPATQKALQR AGLTLQDIGL IELNEAFAAQ SLAVLQEWGL EPEDERLNVN GGAIAIGHPL
GCSGARILTN LVHEMQRRQV QFGLATMCIG VGQGIAMVVE RV
//