ID   INVA3_PAXIN             Reviewed;         949 AA.
AC   A0A0S2E7V8;
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=Inactive atromentin synthetase invA3;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme invA3;
DE            Short=NRPS-like;
GN   Name=invA3;
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: Inactive atromentin synthetase homolog. While the invA3
CC       adenylation (A) domain is capable of adenylating 4-
CC       hydroxyphenylpyruvate (4-HPP), the invA3 enzyme is inactive because of
CC       its non-functional thioesterase (TE) domain.
CC       {ECO:0000269|PubMed:26496685}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.8. {ECO:0000269|PubMed:26496685};
CC       Temperature dependence:
CC         Optimum temperature is 20 degrees Celsius.
CC         {ECO:0000269|PubMed:26496685};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; KT958231; ALN66883.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2E7V8; -.
DR   SMR; A0A0S2E7V8; -.
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..949
FT                   /note="Inactive atromentin synthetase invA3"
FT                   /id="PRO_0000442622"
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..934
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   949 AA;  104373 MW;  9A96F0855E7F00D3 CRC64;
     MTPVAVTSVA PVDIIHDLKR PKRATESSPI TLPDVFSRAV SQYPNHELSF ITSSVHDSSM
     HTTTFTEFNQ RVRALAQAML AWDKPAGAVI VIYLTEHEDN VAAVWACLLS GYVPCLQPAL
     SAQQAHKEGH VAHIKNLFSS ATWLTNESGA EQVQSISGLD IHLLSELKAS AGVGMDFSAH
     QPNPDDEAIL FLTSGSTGFS KAVVHTHRTI LAACHAKGEN YGLTSESKIM NWVGFDHVAG
     SLEMHIAPLL YGASQLHVHV SAILSDPLCF LRLIEENSIQ LAFASNFLLA KLTRDLEKRS
     DLFGKFDLSS IKRINSGGEA VVSSTAQAFA RTLKNLAKDG DASFVISAGF GMTETCAGCI
     YDSINVLETP PSYEFLELGT PVTGCEMRVV NPEDGVTPRP DGESGELQVR GPMVFVRYYN
     NPEATSSSFV EGGWYRTGDV GIVEKGKMRL SGRIKDTVVV HGVSYGIPEL ETYLQTVEGV
     THSFLAAAPY RAPGQETEGF VVFYSPTFGL DSEDAPVKLY ATHCAIRDVS VKLITLPPQQ
     IIPIPINQME RTTLGKLSRA RLVNMFKQGE LAKHIDRAKE LIGIARGASF VALSTETEKT
     LAGIYAVILD LSVGDMSAND NLFELGGTSI DVIRLKREGE SAFDLPEIPT IRILKHPVIS
     NLAKYVDSLV SKDVSEEEYD PIVPLQLTGK KTPIFMVHPG MADVLIFVNL AKYFQNERPF
     YALRARGFEP GQPFFTTTGE IVSCYTAAVK RTQPHGPYAI AGYSYGGVIA FEIAKRLEAM
     GDEVKFTGVI DIIAHRAREN DLTLGLLTLS HLLGLVSKQD INDLAPSMRP LTRKEQLELV
     WKLSPPERLV ELQLTPEKLK HWVNVSGSLM ECGKDYEPAS SVSVMDVFYA NPSRGSKEAW
     LHRLKRWTDY SRSEPSYIDV PGHHYTLMDF DHVARFQKIF RARLEARGL