ID   TR08_CURCL              Reviewed;         311 AA.
AC   A0A348AXY1;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Pyrroline-5-carboxylate reductase-like protein TR08 {ECO:0000303|PubMed:29686660};
DE            EC=1.5.1.- {ECO:0000305|PubMed:29686660};
DE   AltName: Full=KK-1 biosynthesis cluster protein TR08 {ECO:0000303|PubMed:29686660};
DE   Flags: Precursor;
GN   Name=TR08 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135008;
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: Pyrroline-5-carboxylate reductase-like; part of the gene
CC       cluster that mediates the biosynthesis of KK-1, a novel cyclic
CC       decapeptide compound with potent antifungal activity (PubMed:29686660).
CC       The nonribosomal peptide synthetase (NRPS) catalyzes the elongation and
CC       cyclization of the decapeptide chain composed of 1 pipecolic acid
CC       residue (Pip), 1 alanine residue (Ala), 1 aspartic acid residue (Asp),
CC       1 isoleucine residue (Ile), 1 glycine residue (Gly), 1 tyrosine residue
CC       (Tyr) and 4 valine residues (Val) (PubMed:29686660). The Asp, Ile and 3
CC       Val residues are N-methylated by the 5 methyltransferase domains from
CC       the NRPS (found in modules 3, 5, 6, 7 and 9), whereas the Tyr residue
CC       is O-methylated, probably by the cluster encoded O-methyltransferase
CC       OMT (PubMed:29686660). The other tailoring enzymes from the cluster may
CC       be 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 pyrroline-5-carboxylate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; LC371755; BBC83964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AXY1; -.
DR   SMR; A0A348AXY1; -.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01925; P5C_reductase; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645; PTHR11645; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Glycoprotein; NADP; Oxidoreductase; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..311
FT                   /note="Pyrroline-5-carboxylate reductase-like protein TR08"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000450437"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   311 AA;  32897 MW;  9E25C6FAFCF464E3 CRC64;
     MTKRESNTLA VLGCGMVFLV SLLDLANRLL GALGTAILSG ILASMADQTA DDSGRLFTNF
     TACVRRKETG AAVSDKISSH ANANKVEILN KENLRGVKQA DAVLLACQTH LYKALFDEPG
     MREALKKKLI ISVLAGVTTA QLEAALGNGE DYFVIRAMPN IACFVRDSAT VIEKPQRTFP
     EALLHVTDTV FKAVGNVFYI QPSAYDICTA LCGSSPAFLA VFIDSMVDGA VAMGLSHKDA
     VDMAACTMRG AASLVLESGN PWTIRHQVAS PGGSTMQGLL ALEQGNVRST ISNALMVAAK
     EAKKLGSKEN A