TROPG_TALSN
ID TROPG_TALSN Reviewed; 329 AA.
AC B8M9L2;
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=Short-chain dehydrogenase/reductase tropG {ECO:0000303|PubMed:22508998};
DE EC=1.1.1.- {ECO:0000269|PubMed:24863423};
DE AltName: Full=Tropolone synthesis protein G {ECO:0000303|PubMed:24863423};
GN Name=tropG {ECO:0000303|PubMed:24863423};
GN Synonyms=tsR10 {ECO:0000303|PubMed:22508998}; ORFNames=TSTA_117860;
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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of the tropolone class of fungal maleic
CC anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with
CC the 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24863423}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BK008910; DAA64709.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED18014.1; -; Genomic_DNA.
DR RefSeq; XP_002482006.1; XM_002481961.1.
DR AlphaFoldDB; B8M9L2; -.
DR SMR; B8M9L2; -.
DR STRING; 441959.B8M9L2; -.
DR EnsemblFungi; EED18014; EED18014; TSTA_117860.
DR GeneID; 8105844; -.
DR VEuPathDB; FungiDB:TSTA_117860; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_4_1; -.
DR InParanoid; B8M9L2; -.
DR OMA; FMYSLAP; -.
DR OrthoDB; 1076292at2759; -.
DR PhylomeDB; B8M9L2; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..329
FT /note="Short-chain dehydrogenase/reductase tropG"
FT /id="PRO_0000437132"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 24..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 51..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 85..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 178..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 230..232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 329 AA; 36701 MW; B4E13E1964D5412A CRC64;
MVKFFQPKIS PLPDGIDLKG STAVVTGASA GMGLELTRQL LQLNISTVIL AVRNVAKGEN
VVKQLRGDPH IRTYNGNATL KVMELDMDKY DSVQRFAKHL RDEIPIVNFL ILNAGIGLLK
HDRSPSGHDR TLQVNYYSNA LLIAELLPYL KASAERTTIP TRITWVGSRA FETTSLQKTP
LQPNERVLEH MDKKEFFAPF QRYGDSKLLC LLFMCSLARQ IDPKKVIINM LCPGMVNTNM
SDVLPVYLRA VINVVKAIRA RPVEVGVWII LNAALVAGPD SHGKFLIDKD IASESQYISS
PAGQEVQKKI WEETIEELSR LTTLPPEVN
