ID   GREA_SUIGR              Reviewed;         958 AA.
AC   I6NXV7;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Atromentin synthetase greA;
DE            EC=2.3.1.-;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme greA;
DE            Short=NRPS-like;
GN   Name=greA;
OS   Suillus grevillei (Larch bolete) (Boletus elegans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX   NCBI_TaxID=5382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=DSM 8404;
RX   PubMed=22730234; DOI=10.1002/cbic.201200187;
RA   Wackler B., Lackner G., Chooi Y.H., Hoffmeister D.;
RT   "Characterization of the Suillus grevillei quinone synthetase GreA supports
RT   a nonribosomal code for aromatic alpha-keto acids.";
RL   ChemBioChem 13:1798-1804(2012).
CC   -!- FUNCTION: An L-tyrosine:2-oxoglutarate aminotransferase and atromentin
CC       synthetase greA catalyze consecutive steps to turn over L-tyrosine into
CC       atromentin, which represents the generic precursor molecule for the
CC       entire terphenylquinone and pulvinic acid family of pigments, which are
CC       widely distributed secondary metabolites in homobasidiomycetes. The
CC       first step catalyzed by the aminotransferase converts L-tyrosine in to
CC       4-hydroxyphenylpyruvate (4-HPP). Adenylation of two 4-HPP monomers by
CC       the greA adenylation (A) domain, covalent tethering of the monomers as
CC       a thioester and oxoester onto the greA thiolation (T) and thioesterase
CC       (TE) domains, respectively, and symmetric C-C-bond formation between
CC       two monomers catalyzed by the greA TE domain leads to atromentin.
CC       {ECO:0000269|PubMed:22730234}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:22730234};
CC       Temperature dependence:
CC         Optimum temperature is 23 degrees Celsius.
CC         {ECO:0000269|PubMed:22730234};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:22730234}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; JQ681152; AFB76152.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6NXV7; -.
DR   SMR; I6NXV7; -.
DR   BioCyc; MetaCyc:MON-18723; -.
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..958
FT                   /note="Atromentin synthetase greA"
FT                   /id="PRO_0000442627"
FT   DOMAIN          597..675
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          60..465
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          602..672
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          698..946
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         634
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   958 AA;  104883 MW;  71F44FA4E9DDCFC7 CRC64;
     MASIAVTTTT TTTTAEFVTS PRTSIVPEQP NTLHDVIAQA VDSYPLHELG FITSSAHDSS
     IQTKTFSAFN QYVRNLARAM LEWGKPTGSV VVVYLTEHED NMTAVWACLL AGFVPCLQPA
     LSAQQAHKEG HVAHIKNLFG SATWLTSELG AEQINSISGL EVHLLSELKS SAEKFTVAAD
     WVAYEAKPDD EAILFLTSGS TGFSKAVVHT HRTILAACRA KGQSYGLTSE SQVLNWVGFD
     HVAGSLEMHI TPLLYGASQL HVHASAILAD PLRLLRLIDE KSIELAFAPN FLLSKLTRDL
     EKRTDLFGSF DLSSIKRINS GGEAVVSKTA QAFAATMKQL SKNPSAVSFV ISAGFGMTET
     CAGCIYDPVD VLKNKPAHEF LDLGRPINGC EMRIVDPEDG ATLRPDGESG ELQVRGPMVF
     VRYYNNAEAT SSSFVEGGWY RTGDVGIIEN GVMRLSGRIK DTVIVHGVSY GIPELETYLQ
     TVEGVTHSFL AAAPYRAPGQ ETEGFIIFYS PTFDLNGADA STKLFATHRA LRDICVKMIT
     LPPQFVVPIP VNQMEKTTLG KLSRARLISL FKQGQLAQHI ARSEELLSEA RGATFVAPST
     ETEKALAKIY AGIFNLAESE MSASDNFFEL GGTSIDVIRL KREGEAHFGL PEIPTIQILK
     HPVVSSLANY VNALLSKDSQ TEEYDPIVPL QLTGNKTPIF FVHPGVGEVL IFVNLAKYFQ
     NERPFYALRA RGFEPGHPFF TSMDEMVSCY AAAVKRTQAT GPYAIAGYSY GGVVAFEVAK
     RLEAMGDEVK FTGLINIPPH IADRMHEIDW TGGMLNLSYF LGLVSKHDAN DLAPALRPMT
     RNEQLEVVWK LSPPERLVEL QLTPGKLDHW VDIAGSLIEC GKDYNPSGSV SAVDVFYAIP
     LRGSKADWLN NQLKPWSGFS RGDASYTDVP GQHYTLMDFD HVPQFQKIFR GRLEARGL