ID   INVA4_PAXIN             Reviewed;         950 AA.
AC   A0A0S2E7X0;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=Inactive atromentin synthetase invA4;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme invA4;
DE            Short=NRPS-like;
GN   Name=invA4;
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.
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; KT958232; ALN66884.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2E7X0; -.
DR   SMR; A0A0S2E7X0; -.
DR   ESTHER; paxin-inva4; Thioesterase.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43767:SF10; SURFACTIN SYNTHASE SUBUNIT 1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..950
FT                   /note="Inactive atromentin synthetase invA4"
FT                   /id="PRO_0000442623"
FT   DOMAIN          592..670
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          37..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..797
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   950 AA;  105001 MW;  19ED44B082855D6C CRC64;
     MNPVAVTSVA PVDIIHDLRH SEHATEASPI TLLHVFSRAV SQYPNHELNF ITSSAHDSIH
     TKTFTEFDQY VRALAQAMLA WGKPAGSVIV VYLTEHEDNM AAIWASLFAG YVPCLQPALS
     AQQAHKEGHV AHIKNLFSSA TWLTNESGAE QVQSIPGLDI HLLSELQASA ETVSVDFQTH
     QPHLDDEAIL FLTSGSTGFS KAVVHTHRTI LAGCNAKGQS YGLTSESKIM NWVGFDHVVG
     SLGMHITPLL CGASQLHVHA SAILSDSLRF LHLIEEKSIQ LVFAPNFLLA KLTRDLEKRS
     DLFGKFDLSS IKRINSGGEA VVSSTAQAFA RTLKNLAKDG DASFVFSTGF GMTETGAGCI
     YDTIDVLGTS PPHEFLEIGT PVAGCEMRIV NPEDGVTPRP DGESGELQVR GPMVFVRYYN
     NPETTSSSFV EGGWYRTGDV GIFEKGKMRL SGRIKDTVVV HGVSYGIPEL ETYLQTVEGV
     AHSFLVAAPY RAPGQETEGF VVFYSPTFDL DSEDAPAKLY ATHRALRDVS VKLITLPPQQ
     IIPLTLNQME KSTLGKLSRA RLLNLFKQGE LAKYIIRAEE LLGIARGANF VAPSTETEKT
     LAGIYAGIFH LSVSDISTSE NFFEFGGTSI DAIRLKREAE SAFDLSEIPT IQIFKHPEII
     TLAKYVDSLV SKDASEEEYD PIVPLQLTGK KTPIFMVHPG IGEVLIFVNL AKYFQNERPF
     YALRARGFEA GQPCFTSLDE MVSCYAAAIK RTQPHGPYAI AGYSYGGVIA FEVAKRLEVM
     GSEVQFTGII DMIPHHMPRS DWTGGLLILS YFLGLVSKQD TNDLAPSMRP LARTEQFEMV
     WKLSPPERLV ELQLTLEKLE HWVNVADSVR EFAKKYEACS SVSVLDVFYA IPVRGTKEDW
     FNNHIKRWAS YSRAEPSYVD VPGHHYTLMD FDHVPRFQKI FRARLEARGL
//