ID   INVA6_PAXIN             Reviewed;         952 AA.
AC   A0A0S2E7W3;
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 invA6;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme invA6;
DE            Short=NRPS-like;
GN   Name=invA6;
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], AND FUNCTION.
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. Does not accept 4-
CC       hydroxyphenylpyruvate (4-HPP) as substrate. Both the adenylation (A)
CC       and the thioesterase (TE) domain of the invA6 enzyme are inactive.
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; KT958234; ALN66886.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2E7W3; -.
DR   SMR; A0A0S2E7W3; -.
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   2: Evidence at transcript level;
KW   Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..952
FT                   /note="Inactive atromentin synthetase invA6"
FT                   /id="PRO_0000442624"
FT   DOMAIN          594..672
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          58..462
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          599..669
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          695..939
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         631
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   952 AA;  104905 MW;  F34ADAA38456A05A CRC64;
     MAPVAITPAT LVGHDLKSSR ASERATELSP VTLLDIFSRA VSLYPKHELS FVTSSAHDSS
     VQTRSFSEFD QYARALAWAM LAWGKPTGSV IVVYFTEHED NMAAVWACLL AGHVPCLQPA
     LSEQQAHKEG HVAHIKNLFS SATWLTNESG AEQVHSITGL DIRLLSELKA RAETVGADFH
     AHQPNPDDEA ILFLTSGSTG FSKVVVHTHR TILAACNAKG QSYGLTSESK TMNWVGFDHV
     AGSLEMHIAP LLYGASQLHV HVSAILADPS RFLRLIEEKS IQLAFAPNFL LAKLTRDLEK
     CSDLFGKFDL SSIKRINSGG EAVVSSTAQA FARTLKNFAK DGNASFVISA GFGTTETCAG
     CIYDPIDVLF TPPSYEFLEL GTPLTGCEMC IVNPQDGVTP RPDGESGELQ VRGPMVFVRY
     YNDPKATTSS FIEGVWYRTG DVGIIEKGKM RLNGRIKDTV IVHGVSYGIA ELETYLQTVE
     GVTHSFLAAA PHRDPGQETE GFVIFYSPTF ELDSEDAPAK LYATHRALRD VSVKMITLPP
     QQIIPIPLNQ MEKTTLGKLS RVCLVNLFKQ GELANHIARA EELLSIARGA TFIAPSTETE
     KTLGRLYAEI FNLRVSDVSA SDNFFELGGN SIDVIKLKRE AESLFELPEI LTVQILKHPV
     ISSLAKYVDS LVSKDGSQEE YDPVVPLQLT SNKTPIFMVH PGIGEVLAYV DLAKYFQNER
     PFFALRVRGF EGQPLFTSMD EMASSYAAGA KRTQPHGPYA IAGYSYGGVV AFEVAKRLES
     MGDEVKFIGL VDIPPHIADR MHDWTSGMLN LSHLLGLMSK QDADNLAPSL RTLTRKEQFE
     VLWKLSPPER LTELQLTPEK HENWVYIAGG LSECGMTYQP GGSVSVLDVF YAMPPHDTKE
     DWLNQHLRRW ADFCRSEPSF TNVPGHHDTL MDFDHVSGFQ KIFRDALEAR GL