ID   TR07_CURCL              Reviewed;         348 AA.
AC   A0A348AXY0;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Probable dehydrogenase TR07 {ECO:0000303|PubMed:29686660};
DE            EC=1.1.1.- {ECO:0000305|PubMed:29686660};
DE   AltName: Full=KK-1 biosynthesis cluster protein TR07 {ECO:0000303|PubMed:29686660};
GN   Name=TR07 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135007;
OS   Curvularia clavata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=95742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=BAUA-2787;
RX   PubMed=29686660; DOI=10.3389/fmicb.2018.00690;
RA   Yoshimi A., Yamaguchi S., Fujioka T., Kawai K., Gomi K., Machida M.,
RA   Abe K.;
RT   "Heterologous Production of a Novel Cyclic Peptide Compound, KK-1, in
RT   Aspergillus oryzae.";
RL   Front. Microbiol. 9:690-690(2018).
CC   -!- FUNCTION: Probable dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of KK-1, a novel cyclic decapeptide compound
CC       with potent antifungal activity (PubMed:29686660). The nonribosomal
CC       peptide synthetase (NRPS) catalyzes the elongation and cyclization of
CC       the decapeptide chain composed of 1 pipecolic acid residue (Pip), 1
CC       alanine residue (Ala), 1 aspartic acid residue (Asp), 1 isoleucine
CC       residue (Ile), 1 glycine residue (Gly), 1 tyrosine residue (Tyr) and 4
CC       valine residues (Val) (PubMed:29686660). The Asp, Ile and 3 Val
CC       residues are N-methylated by the 5 methyltransferase domains from the
CC       NRPS (found in modules 3, 5, 6, 7 and 9), whereas the Tyr residue is O-
CC       methylated, probably by the cluster encoded O-methyltransferase OMT
CC       (PubMed:29686660). The other tailoring enzymes from the cluster may be
CC       involved in further modifications leading to the synthesis of KK-1
CC       (Probable). {ECO:0000269|PubMed:29686660, ECO:0000305|PubMed:29686660}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29686660}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; LC371755; BBC83963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AXY0; -.
DR   SMR; A0A348AXY0; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; NAD; Oxidoreductase.
FT   CHAIN           1..348
FT                   /note="Probable dehydrogenase TR07"
FT                   /id="PRO_0000450436"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        298
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         158..159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         208..209
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         235..237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
SQ   SEQUENCE   348 AA;  38200 MW;  7B57BFED509EB41E CRC64;
     MKLTVFSAKP YDIEYLGGIA TNQNSSPAIE INFLHVPLSS ETAAFANGAD AVCVFVHDVL
     DANVLRELYA AGVRAILFRC SGYNNIDLRE AERLGFFVAN VPSYSPEAVA EFAVALIQTL
     NRKTHRAYNR VRDGNFNLDG LLGRTLHGKT VGIVGSGRIG LAMAQIVQGF GCKLLAYDPR
     PTEAFKKYGE YVDLDTLLSQ CDIVSLHCPL MDSTQHIIND TTVSKMKRGA MLVNTSRGGL
     IDTQSVMKAL KSKRLGGLAL DVYEGERALF YKDHSGDIIH DDLLMRLTTF HNVVVSGHQA
     YFTEEALTEI AECTLRNLDD WAKGVPTANA LVQGRNSNGR RERGLARL