TROPJ_TALSN
ID TROPJ_TALSN Reviewed; 266 AA.
AC B8M9J5;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Decarboxylase tropJ {ECO:0000303|PubMed:22508998};
DE EC=1.-.-.- {ECO:0000269|PubMed:22508998};
DE AltName: Full=Tropolone synthesis protein J {ECO:0000303|PubMed:24863423};
GN Name=tropJ {ECO:0000303|PubMed:24863423};
GN Synonyms=tsL3 {ECO:0000303|PubMed:22508998}; ORFNames=TSTA_117720;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=22508998; DOI=10.1073/pnas.1201469109;
RA Davison J., al Fahad A., Cai M., Song Z., Yehia S.Y., Lazarus C.M.,
RA Bailey A.M., Simpson T.J., Cox R.J.;
RT "Genetic, molecular, and biochemical basis of fungal tropolone
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7642-7647(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=24863423; DOI=10.1002/anie.201403450;
RA al Fahad A., Abood A., Simpson T.J., Cox R.J.;
RT "The biosynthesis and catabolism of the maleic anhydride moiety of
RT stipitatonic acid.";
RL Angew. Chem. Int. Ed. 53:7519-7523(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Decarboxylase; part of the gene cluster that mediates the
CC biosynthesis of the tropolone class of fungal maleic anhydrides
CC (PubMed:22508998, PubMed:24863423). The pathway begins with the
CC synthesis of 3-methylorcinaldehyde by the non-reducing polyketide
CC synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the
CC substrate for the FAD-dependent monooxygenase tropB to yield a
CC dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423).
CC The 2-oxoglutarate-dependent dioxygenase tropC then performs the
CC oxidative ring expansion to provide the first tropolone metabolite
CC stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts
CC stipitaldehyde into stipitacetal which is in turn converted to
CC stipitalide by the short-chain dehydrogenase/reductase tropE
CC (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI
CC and tropJ to form successive tropolone maleic anhydrides including
CC stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423).
CC {ECO:0000269|PubMed:22508998, ECO:0000269|PubMed:24863423}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0AB87};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0AB87};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24863423}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. {ECO:0000305}.
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DR EMBL; BK008910; DAA64702.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED17997.1; -; Genomic_DNA.
DR RefSeq; XP_002481989.1; XM_002481944.1.
DR AlphaFoldDB; B8M9J5; -.
DR SMR; B8M9J5; -.
DR STRING; 28564.XP_002481989.1; -.
DR PRIDE; B8M9J5; -.
DR EnsemblFungi; EED17997; EED17997; TSTA_117720.
DR GeneID; 8105830; -.
DR VEuPathDB; FungiDB:TSTA_117720; -.
DR eggNOG; ENOG502SKYK; Eukaryota.
DR HOGENOM; CLU_006033_2_2_1; -.
DR InParanoid; B8M9J5; -.
DR OMA; NTIHMAG; -.
DR OrthoDB; 1105691at2759; -.
DR PhylomeDB; B8M9J5; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 3: Inferred from homology;
KW Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..266
FT /note="Decarboxylase tropJ"
FT /id="PRO_0000437136"
FT ACT_SITE 80
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ SEQUENCE 266 AA; 29391 MW; FD838AB4649E3026 CRC64;
MNLPASIPVR TFISGCHILH RHHVLDAYGH LSVRNPERSD TFFMSRDLAP GLISSSVDLV
EYFVHDASPV NPASPAGYIE RFIHSEIYQK YPEVQSVVHS HASTVLPYTI TGVNLRPCVH
MSGFLGASVP NFDVAKFYKE DDKCDLLIRN KDLGAHLAEC FSAPESDSES TRSVVLMRGH
GFTAVGGSIP ESVYRAIYTV ENAKIQTVSM TLSAAAAKGD GPHSGIYFLP EHEIRGTKEL
TQRSVMRSWK LWVREVETGG LYTNLA
