ID   INVA1_PAXIN             Reviewed;         959 AA.
AC   A0A0S2E7Z1;
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 invA1;
DE            EC=2.3.1.-;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme invA1;
DE            Short=NRPS-like;
GN   Name=invA1;
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 invA1 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 invA1 adenylation (A) domain, covalent
CC       tethering of the monomers as a thioester and oxoester onto the invA1
CC       thiolation (T) and thioesterase (TE) domains, respectively, and
CC       symmetric C-C-bond formation between two monomers catalyzed by the
CC       invA1 TE domain leads to atromentin. {ECO:0000269|PubMed:26496685}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2. {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; KT958230; ALN66882.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2E7Z1; -.
DR   SMR; A0A0S2E7Z1; -.
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..959
FT                   /note="Atromentin synthetase invA1"
FT                   /id="PRO_0000442620"
FT   DOMAIN          598..676
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          59..466
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          603..673
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          699..946
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         635
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   959 AA;  104854 MW;  D63FA6BECECA6D43 CRC64;
     MSPVATTTSV TPDVISSLKT SFSAGQTSYI PSTLFDVLSY AAERYPSHEL GFITSSAHDS
     SIQTKTFSLF NAQVRNLGRA LLDLNKPAGS IIVVYLTEHE DNMAAVWACL LAGYVPCLQP
     ALSAQQAHKE GHVAHIKNLF GSATWLTNEA GAEQVSSIAG LEIHLLSELK IAAEGYSVSA
     DWTARTVQPD DEAILFLTSG STGFSKAVVH THRTILAACY AKGEAYGLTS ESNILNWVGF
     DHVAGSLEMH IAPLLYGASQ LHVHASAILS DPLRFLQLID EKSINVAFAP NFLLAKLTRD
     LEKKTELFGS FDLSSVTRIN SGGEAVVSKT AKAFVATLKN LSRDPSKVSF VISPGFGMTE
     TCAGCIYNPA DVSTSEPNYE FLELGTPITG CEMRIVNPED GVTPRVDGES GELQVRGPMV
     FSRYYNNAEA TASSFVEGGW YRTGDVGIVE NGVMRLSGRI KETVIVHGVS YGIPELETYL
     QTVEGVTHSF LAAAPYRAPG QETEGFIIFY APTFDLYGED ASSKLFATHR ALRDISVKMI
     TLPPQHIVPI PVNQMEKTTL GKLSRARLTG LFKQGELAKH IARAEELLSE ARGASFVTPQ
     TETEQTLAAI YAGIFNLEVA DVSATDNFFE LGGTSIDVIR LKREGEAAFD LPEIPTIQIL
     KHPVVSSLAN YIVALKTKGV NAEEYDPIVP LQLTGKKTPI FMVHPGVGEV LIFVNLAKYF
     QNERPFYALR ARGFEPGQPF FTSMDEMVSC YAAAVKRTQA HGPYAIAGYS YGGVVAFEVA
     KRLEAMGEEV KFTGLINIPP HIADRMHEID WTGGMLNLSY FLGLVSKQDA NDLAPSMRPL
     TRKEQLEIVW KLSPPERLVE LQLTPEKLDH WVDIAGSLIE CGKEYNPGGS VSALDVFYAI
     PLRGSKEDWL NKQLKPWEEF SRGATSYTDV PGQHYTLMDF DHVPGFQKIF RSRLEARGL