ID   THNC_TRIHA              Reviewed;         320 AA.
AC   A0A0F9ZXE3;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=2-oxoglutarate-dependent dioxygenase thnC {ECO:0000303|PubMed:33570538};
DE            EC=1.14.11.- {ECO:0000269|PubMed:33570538};
DE   AltName: Full=Trihazone biosynthesis cluster protein C {ECO:0000303|PubMed:33570538};
GN   Name=thnC {ECO:0000303|PubMed:33570538}; ORFNames=THAR02_03177;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776;
RX   PubMed=26067977; DOI=10.1128/genomea.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=33570538; DOI=10.1039/d0ob02545c;
RA   Zhu Y., Wang J., Mou P., Yan Y., Chen M., Tang Y.;
RT   "Genome mining of cryptic tetronate natural products from a PKS-NRPS
RT   encoding gene cluster in Trichoderma harzianum t-22.";
RL   Org. Biomol. Chem. 19:1985-1990(2021).
CC   -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC       cluster that produces the tetronate natural products trihazones
CC       (PubMed:33570538). ThnC catalyzes the oxidative decarboxylation of
CC       trihazone A to trihazone D (PubMed:33570538). The C4 hydrogen is first
CC       abstracted by the iron-oxo species generated in ThnC to give a tertiary
CC       radical at C4 (PubMed:33570538). This is followed by decarboxylation
CC       and removal of the second electron by the FeIII-OH center to give
CC       trihazone D (PubMed:33570538). The pathway begins with the formation of
CC       trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl
CC       reductase thnE. Trihazone A is further decarboxylated by the 2-
CC       oxoglutarate-dependent dioxygenase thnC to produce trihazone D. The
CC       function of the FAD-dependent monooxygenase thnD has still to be
CC       identified (PubMed:33570538). {ECO:0000269|PubMed:33570538}.
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:33570538}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JOKZ01000069; KKP04697.1; -; Genomic_DNA.
DR   EnsemblFungi; KKP04697; KKP04697; THAR02_03177.
DR   OMA; GRTIWEI; -.
DR   OrthoDB; 755305at2759; -.
DR   Proteomes; UP000034112; 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   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..320
FT                   /note="2-oxoglutarate-dependent dioxygenase thnC"
FT                   /id="PRO_0000455678"
FT   DOMAIN          174..278
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         199
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         258
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         268
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   320 AA;  36311 MW;  616C20C26B3AEEA6 CRC64;
     MSEEDISLPI IDLSGYLSPK SPDDRQNVIE QIRDACRDFG FFQLKGHGIP ISLQKELLKS
     LGTLFSMPKE EKMKLSYLEN PCRRGYEASG MSMREGDAMP DSKEAYYLGR EDPVVEFSGF
     YGPNVWPNLP EEDFRGPVWE YYQKTSQLGK TIWEVLLQGL GYSTDLMEAF AKRPLVQMKL
     IRYPSPSVTL PGQFGVGAHN DFGGVTVLLQ QAGKDGLEVW LEKQQKWLSV PALEDVYVIN
     CGDMIMKWSG GRYKSVRHRV INKTEGERHS CATFWHGDVF ATNPLNPEDP NKETVGQLLV
     KRFRHQMSIH KEGLAQVGEL