TROPC_TALSN
ID TROPC_TALSN Reviewed; 325 AA.
AC B8M9K5;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase tropC {ECO:0000303|PubMed:22508998};
DE EC=1.14.-.- {ECO:0000269|PubMed:22508998};
DE AltName: Full=Tropolone synthesis protein C {ECO:0000303|PubMed:22508998};
GN Name=tropC {ECO:0000303|PubMed:22508998};
GN Synonyms=tsR5 {ECO:0000303|PubMed:22508998}; ORFNames=TSTA_117800;
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], FUNCTION, DISRUPTION PHENOTYPE, AND
RP CATALYTIC ACTIVITY.
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].
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: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC cluster that mediates the biosynthesis of the tropolone class of fungal
CC maleic anhydrides (PubMed:22508998, PubMed:24863423). The pathway
CC begins with the synthesis of 3-methylorcinaldehyde by the non-reducing
CC polyketide synthase (PKS) tropA (PubMed:22508998). 3-
CC methylorcinaldehyde is the substrate for the FAD-dependent
CC monooxygenase tropB to yield a dearomatized hydroxycyclohexadione
CC (PubMed:22508998, PubMed:24863423). The 2-oxoglutarate-dependent
CC dioxygenase tropC then performs the oxidative ring expansion to provide
CC the first tropolone metabolite stipitaldehyde (PubMed:22508998,
CC PubMed:24863423). Trop D converts stipitaldehyde into stipitacetal
CC which is in turn converted to stipitalide by the short-chain
CC dehydrogenase/reductase tropE (PubMed:24863423). The next steps involve
CC tropF, tropG, tropH, tropI and tropJ to form successive tropolone
CC maleic anhydrides including stipitaldehydic, stipitatonic and
CC stipitatic acids (PubMed:24863423). {ECO:0000269|PubMed:22508998,
CC ECO:0000269|PubMed:24863423}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22508998}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of tropolones but leads to
CC the accumulation of talaroenamine (PubMed:22508998).
CC {ECO:0000269|PubMed:22508998}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; BK008910; DAA64706.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED18007.1; -; Genomic_DNA.
DR RefSeq; XP_002481999.1; XM_002481954.1.
DR PDB; 6XJJ; X-ray; 2.70 A; A=1-325.
DR PDBsum; 6XJJ; -.
DR AlphaFoldDB; B8M9K5; -.
DR SMR; B8M9K5; -.
DR STRING; 28564.XP_002481999.1; -.
DR EnsemblFungi; EED18007; EED18007; TSTA_117800.
DR GeneID; 8105838; -.
DR VEuPathDB; FungiDB:TSTA_117800; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_3_1; -.
DR InParanoid; B8M9K5; -.
DR OMA; NGHETEV; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; B8M9K5; -.
DR BioCyc; MetaCyc:MON-19388; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..325
FT /note="2-oxoglutarate-dependent dioxygenase tropC"
FT /id="PRO_0000437129"
FT DOMAIN 185..287
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 278
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6XJJ"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:6XJJ"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 142..171
FT /evidence="ECO:0007829|PDB:6XJJ"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:6XJJ"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6XJJ"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:6XJJ"
SQ SEQUENCE 325 AA; 36226 MW; 5F2902CE9A5B461B CRC64;
MSIGDEVIPT VDISAWLSST ASPESKNKVV EEVRSACNKY GFFNLVGHGI PAEAREKIFG
CTKKFFDLPL EEKMKISVDK SLGKSFRGYE PSLIQTHQDG LLPDTKECFI TGAEIPADHP
DAGKFSTGPN LWPEGLSDKE FRQPVMEYRA LMLDLVSTIV RILGQGIHKA FGHPSDVLND
ILINPSIPMR LLHYAPQENP DPRQFGVGDH TDFGCVSILL QQKGTKGLEV WYPPKETWIP
VPVIEDAFVI NMGDTMHRWT GGYYRSARHR VYITGERRYS VAFFLNGNLN LKIKPLDGSG
GEASVGEHIN SRLAHTLGDN AKYLR
