ID   ATR10_STAC4             Reviewed;         276 AA.
AC   A0A084R1I4;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Short-chain dehydrogenase/reductase ATR10 {ECO:0000303|PubMed:25015739};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE   AltName: Full=Core atranone cluster (CAC) protein 10 {ECO:0000303|PubMed:25015739};
GN   Name=ATR10 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03335;
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP   FUNCTION.
RC   STRAIN=IBT 40285;
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- FUNCTION: Short-chain dehydrogenase/reductase; part of the core
CC       atranone cluster (CAC) which products are predicted to catalyze most or
CC       all steps of mycotoxin atranone synthesis, starting from geranylgeranyl
CC       pyrophosphate (GGPP) (PubMed:25015739). The initial cyclization of GGPP
CC       to dolabellane is probably performed by the terpene cyclase ATR13
CC       (PubMed:25015739). The Baeyer-Villiger oxidation near the end of the
CC       atranone synthesis, which converts atranones D and E to atranones F and
CC       G is predicted to be catalyzed by the monooxygenase ATR8
CC       (PubMed:25015739). Of the CAC's other predicted gene products, the
CC       reducing PKS ATR6 might synthesize a polyketide chain
CC       (PubMed:25015739). This polyketide is probably transferred onto the
CC       atranone backbone by the polyketide transferase ATR5 (By similarity).
CC       Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4,
CC       and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a
CC       methyltransferase (ATR12) (PubMed:25015739). These may all be involved
CC       in the various steps of atranone biosynthesis, although their specific
CC       roles must await experimental determination (PubMed:25015739).
CC       {ECO:0000250|UniProtKB:Q4WAY4, ECO:0000305|PubMed:25015739}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
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; KL659308; KFA70069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084R1I4; -.
DR   SMR; A0A084R1I4; -.
DR   EnsemblFungi; KFA70069; KFA70069; S40285_03335.
DR   HOGENOM; CLU_010194_9_0_1; -.
DR   OMA; NYHIIIG; -.
DR   OrthoDB; 1259665at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase 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   Monooxygenase; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Short-chain dehydrogenase/reductase ATR10"
FT                   /id="PRO_0000442406"
FT   BINDING         21..29
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         48..50
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         77..79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         179..183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         212..214
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   276 AA;  29822 MW;  6E809A8EC47E4A07 CRC64;
     MARQSAEPPT DDGQSAKEIV VITGGNTGIG FEVARQLLCN YGNRFYVIIG SRTLGKGHTA
     VAALKQQGYE AVQAVQLDVT KEASIAAAAK IIGEQFGRID VLHVNAGVLL EPTDINAKPV
     PFSETIMETM RTNVAGAAAT VEGFTPLLSI GSNPRVVFMT STAASAQLMH QYSSMTTAPA
     LSASKAAENI IMIYYYHKYP NWKVNACYPG YRDTAMMRRY NASSLSKAYR QPDPVEEGAY
     NAVRLSLLGK DGETGTFTEY KGVGEDGQRQ YSALPW