ID   INVA5_PAXIN             Reviewed;         953 AA.
AC   A0A0S2E7W7;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Atromentin synthetase invA5;
DE            EC=2.3.1.-;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme invA5;
DE            Short=NRPS-like;
GN   Name=invA5;
OS   Paxillus involutus (Naked brimcap).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=71150;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC MYA-4647;
RX   PubMed=26496685; DOI=10.1016/j.chembiol.2015.08.016;
RA   Braesel J., Gotze S., Shah F., Heine D., Tauber J., Hertweck C., Tunlid A.,
RA   Stallforth P., Hoffmeister D.;
RT   "Three redundant synthetases secure redox-active pigment production in the
RT   basidiomycete Paxillus involutus.";
RL   Chem. Biol. 22:1325-1334(2015).
CC   -!- FUNCTION: An L-tyrosine:2-oxoglutarate aminotransferase (probably invD)
CC       and atromentin synthetase invA5 catalyze consecutive steps to turn over
CC       L-tyrosine into atromentin, which represents the generic precursor
CC       molecule for the entire terphenylquinone and pulvinic acid family of
CC       pigments, which are widely distributed secondary metabolites in
CC       homobasidiomycetes. The first step catalyzed by the aminotransferase
CC       converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP). Adenylation
CC       of two 4-HPP monomers by the invA5 adenylation (A) domain, covalent
CC       tethering of the monomers as a thioester and oxoester onto the invA5
CC       thiolation (T) and thioesterase (TE) domains, respectively, and
CC       symmetric C-C-bond formation between two monomers catalyzed by the
CC       invA5 TE domain leads to atromentin. {ECO:0000269|PubMed:26496685}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.4. {ECO:0000269|PubMed:26496685};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:26496685};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000250|UniProtKB:B7STY1}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; KT958233; ALN66885.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2E7W7; -.
DR   SMR; A0A0S2E7W7; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   1: Evidence at protein level;
KW   Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..953
FT                   /note="Atromentin synthetase invA5"
FT                   /id="PRO_0000442625"
FT   DOMAIN          592..670
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          37..460
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          597..667
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          693..795
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         629
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   953 AA;  104609 MW;  531CBAC5B156DF29 CRC64;
     MTPIAITPVA PVDIIYDLKH TERATESSPV TLLDVFSRAV SQYPDHELSF ITSSAHDSTV
     HTKTFAEFNQ HVHALAQAMR AWGKPTGSVI VVYLTEHEDN MAAVWASLLA GYVPCLQPAL
     SAQQAHKEGH VGHIKNLFSS ATWLTNESGA EQVQSISGLD IHLLSELKAS AEAGVDFQAH
     QPNPDDEAIL FLTSGSTGFS KAVVHTHRTI LAACHAKGES YGLTSESKIM NWVGFDHVAG
     SLEMHIAPLL YGASQLHVHA SAILSDPLRF LHLIEEKSIQ LAFAPNFLLA KLTRDLEKRS
     DLFGKFDLSS IKRINSGGEA VVSSTAQAFA RTLQNLAKDG DASFVISAGF GMTETCAGCI
     YDPINVLETP PSYEFLELGT PVAGCEMRIV NPEDGVTPRP DGESGELQVR GPMVFVRYYN
     NPEATSSSFV EGGWYRTGDV GIVEQGKMRL SGRIKDTVIV HGVSYGIPEL ETYLQTVEGV
     THSFLAAAPY RAPGQETEGF VVFYSPTFDL DSEDAPAKLF ATHRALRDVS VKLITLPPQQ
     IIPIPINQME KTTLGKLSRA RLVNLLKQGE LAKHIDRAEE LVSIARGASF VAPSTETEKT
     LAGIYAGIFN LSVSDMSASE NFFELGGTSI DVIRLKREGE SAFDLPEIPT IQILKHPVIS
     SLAKYVDSLI SKDASQEEYD PIVPLQLTGN KTPIFMVHPG VGEVLIFVNL AKYFQNERPF
     YALRARGFEP GHPFFTTMDE MVSCYAAAVK RTQPHGPYAI AGYSYGGVVA FEVAKRLEAM
     GDEVKFTGLI NIPPNIADRM HEIDWTGGML NLSYFLGLVS KQDANDLAPS MRPLTRKEQL
     EIVWKLSPPE RLVELQLTPE KLDHWVDIAG SLIECGKTYE PGSSVSVLDV FYAIPLRGSK
     EDWLNKQLKP WAGYSRAEPS YTDVPGQHYT LMDFDHVPGF QKIFRSRLEA RGL