ID   INVA2_PAXIN             Reviewed;         953 AA.
AC   A0A0S1RUN4;
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 invA2;
DE            EC=2.3.1.-;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme invA2;
DE            Short=NRPS-like;
GN   Name=invA2;
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 [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   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 invA2 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 invA2 adenylation (A) domain, covalent
CC       tethering of the monomers as a thioester and oxoester onto the invA2
CC       thiolation (T) and thioesterase (TE) domains, respectively, and
CC       symmetric C-C-bond formation between two monomers catalyzed by the
CC       invA2 TE domain leads to atromentin. {ECO:0000269|PubMed:26496685}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.6. {ECO:0000269|PubMed:26496685};
CC       Temperature dependence:
CC         Optimum temperature is 20 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; KT935508; ALL98445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S1RUN4; -.
DR   SMR; A0A0S1RUN4; -.
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 invA2"
FT                   /id="PRO_0000442621"
FT   DOMAIN          592..670
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          38..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;  104561 MW;  CC06EF181AA04025 CRC64;
     MTPIAVTPVA PVDIIYDLKH TERATESSPV TLLDVFSRAV SQYPNHELSF ITSSAHDSTI
     HTKTFAEFNQ DVHALAQAMR AWGKPTGSVI VVYLTEHEDN MAAVWASLLA GYVPCLQPAL
     SAQQAHKEGH VGHIKNLFSS ATWLTNESGA EQVQSISGLD IHLLSELKAS AEAGVDFQAH
     QPNSDDEAIL FLTSGSTGFS KAVVHTHRTI LAACHAKGES YGLTSESKIM NWVGFDHVAG
     SLEMHIAPLL YGASQLHVHA SAILSDPLRF LHLIEEKSIQ LAFAPNFLLA KLTRDLEKRS
     DLFGKFDLSS IKRINSGGEA VVSSTAQAFA RTLKNLAKDG DASFVISAGF GMTETCAGCI
     YDPINVLETP PSYEFLELGT PVAGCEMRVV NPEDGVTPRP DGESGELQVR GPMVFVRYYN
     NPEATSSSFV EGGWYRTGDV GIVEQGKMRL SGRIKDTVIV HGVSYGIPEL ETYLQTVEGV
     THSFLAAAPY RAPGQETEGF VVFYSPTFDL DSEDAPAKLF ATHRALRDVS VKLITLPPQQ
     IIPIPINQME KTTLGKLSRA RLVNLFKQGE LAKHIDRAEE LVSIARGASF VAPSTETEKT
     LAGIYAGIFN LSVGDMSASE NFFELGGTSI DVIRLKREGE SAFDLPEIPT IQILKHPVIS
     SLAKYVDSLI SKDASQEEYD PIVPLQLTGN KTPIFMVHPG VGEVLIFVNL AKYFQNERPF
     YALRARGFEP GHPFFTTMDE MVSSYAAAIK RTQAHGPYAI AGYSYGGVVA FEVAKRLEAM
     GDEVKFTGLI NIPPHIADRM HEIDWTGGML NLSYFLGLVS KQDANDLAPS MRPLTRKEQL
     EIVWKLSPPE RLVELQLTPE KLDHWVDIAG SLIECGKTYE PASSVSVLDV FYAIPLRGSK
     EDWLNNQLKP WAGYSRAEPS YTDVPGQHYT LMDFDHVPGF QKIFRSRLEA RGL