ID   TR02_CURCL              Reviewed;         538 AA.
AC   A0A348AXX5;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Putative amidase {ECO:0000303|PubMed:29686660};
DE            EC=3.5.1.4 {ECO:0000305|PubMed:29686660};
DE   AltName: Full=KK-1 biosynthesis cluster protein TR02 {ECO:0000303|PubMed:29686660};
GN   Name=TR02 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF068002;
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: Putative amidase; part of the gene cluster that mediates the
CC       biosynthesis of KK-1, a novel cyclic decapeptide compound with potent
CC       antifungal activity (PubMed:29686660). The nonribosomal peptide
CC       synthetase (NRPS) catalyzes the elongation and cyclization of the
CC       decapeptide chain composed of 1 pipecolic acid residue (Pip), 1 alanine
CC       residue (Ala), 1 aspartic acid residue (Asp), 1 isoleucine residue
CC       (Ile), 1 glycine residue (Gly), 1 tyrosine residue (Tyr) and 4 valine
CC       residues (Val) (PubMed:29686660). The Asp, Ile and 3 Val residues are
CC       N-methylated by the 5 methyltransferase domains from the NRPS (found in
CC       modules 3, 5, 6, 7 and 9), whereas the Tyr residue is O-methylated,
CC       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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC         NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC         Evidence={ECO:0000305|PubMed:29686660};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29686660}.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; LC371755; BBC83958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AXX5; -.
DR   SMR; A0A348AXX5; -.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Hydrolase.
FT   CHAIN           1..538
FT                   /note="Putative amidase"
FT                   /id="PRO_0000450434"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   ACT_SITE        233
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
SQ   SEQUENCE   538 AA;  59111 MW;  3910DE8380E50882 CRC64;
     MTEPTWKTVA SEKQQQRESK IPSEWQIPKS SHPAPEVTFV QDFPAKSGMF TNRELQLTAA
     TASDVTAKIS TGEWTAVEVT TAVCKRAAVA QQLLNCVTEI CFDQAIARAK ELDAYFEKEG
     KTVGPLHGLP ISFKDQFNVK GFDSTIGYCS YASKPATADS TLVKLLVKAG AIIYVKSNVP
     ITLMMGESFN NIFGRTLNPR NRELTTGGSS GGEAALVTFC ASFLGVGTDI GGSLRIPCSF
     TGLYGLRPSH GRVSYQHVQN TLLGQEAVRS CAGPMCRAPE DIRLFMSSLA AQQPWLWDPQ
     SLPLPWRAEE EVLPKKLCFG FALGDGHVGP KKLKQAGHAV INFNLTEGKE VNEIMNKMFT
     ADGGAEFQRD TDATGEPLPP TVEYWLGHSS QIKASTVSET WKNQHKKALL AQKFLEKWQA
     TKGRTGTSRP IDGLIMPSTP FPASRHGSGW PWHFGDLSAL LDLTTGVFPV TRVNLEKDAV
     PPSWTPMSVK DKEAMDYYEK PENHENALVG LQLIGRRLEE EKVTAMLTLI RNVLEVDY