ID   ATR7_STAC4              Reviewed;         320 AA.
AC   A0A084R1K1;
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 ATR7 {ECO:0000303|PubMed:25015739};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE   AltName: Full=Core atranone cluster (CAC) protein 7 {ECO:0000303|PubMed:25015739};
GN   Name=ATR7 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03332;
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}.
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DR   EMBL; KL659308; KFA70086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084R1K1; -.
DR   SMR; A0A084R1K1; -.
DR   EnsemblFungi; KFA70086; KFA70086; S40285_03332.
DR   HOGENOM; CLU_010194_13_1_1; -.
DR   OMA; KGTMNTL; -.
DR   OrthoDB; 1053465at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..320
FT                   /note="Short-chain dehydrogenase/reductase ATR7"
FT                   /id="PRO_0000442404"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         26..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         53..56
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         105..107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         209..213
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         240..242
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   320 AA;  34765 MW;  EEAD111ADE62E17B CRC64;
     MSTLTIDPTS IPPLEGKTAV VTATPLVPGG ASGIGLAAAK IMLQKGATVY ALDRQEPIEA
     VPGLKFRRCD VTSWSALREV FDEIQQVHLA FANAGICDKS PESYYDDVCD NGNLQEPDYS
     MIDVNLKAVL NFVKLARHSM RRHQVQGSIV ITASSTGLVP EQSAPVYSST KFAVIGLVRT
     LRSVLIQENI TINAVAPFVT TTGMAPAEAM VPLKNLGVQT SPADFVGLAL VYSAVARQTR
     RVEAYGKETE EDILEHGRWN GRVILTLGDK YTEVEEEFSK SRPLWTGGEV LQSIRLQQAV
     LDFRHGGVAI KSNRPSNQLN