ID INVA5_PAXIN Reviewed; 953 AA.
AC A0A0S2E7W7;
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=Atromentin synthetase invA5;
DE EC=2.3.1.-;
DE AltName: Full=Nonribosomal peptide synthase-like enzyme invA5;
DE Short=NRPS-like;
GN Name=invA5;
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 invA5 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 invA5 adenylation (A) domain, covalent
CC tethering of the monomers as a thioester and oxoester onto the invA5
CC thiolation (T) and thioesterase (TE) domains, respectively, and
CC symmetric C-C-bond formation between two monomers catalyzed by the
CC invA5 TE domain leads to atromentin. {ECO:0000269|PubMed:26496685}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4. {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; KT958233; ALN66885.1; -; mRNA.
DR AlphaFoldDB; A0A0S2E7W7; -.
DR SMR; A0A0S2E7W7; -.
DR ESTHER; paxin-inva5; Thioesterase.
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; 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; 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 1: Evidence at protein level;
KW Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..953
FT /note="Atromentin synthetase invA5"
FT /id="PRO_0000442625"
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..795
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 953 AA; 104609 MW; 531CBAC5B156DF29 CRC64;
MTPIAITPVA PVDIIYDLKH TERATESSPV TLLDVFSRAV SQYPDHELSF ITSSAHDSTV
HTKTFAEFNQ HVHALAQAMR AWGKPTGSVI VVYLTEHEDN MAAVWASLLA GYVPCLQPAL
SAQQAHKEGH VGHIKNLFSS ATWLTNESGA EQVQSISGLD IHLLSELKAS AEAGVDFQAH
QPNPDDEAIL FLTSGSTGFS KAVVHTHRTI LAACHAKGES YGLTSESKIM NWVGFDHVAG
SLEMHIAPLL YGASQLHVHA SAILSDPLRF LHLIEEKSIQ LAFAPNFLLA KLTRDLEKRS
DLFGKFDLSS IKRINSGGEA VVSSTAQAFA RTLQNLAKDG DASFVISAGF GMTETCAGCI
YDPINVLETP PSYEFLELGT PVAGCEMRIV NPEDGVTPRP DGESGELQVR GPMVFVRYYN
NPEATSSSFV EGGWYRTGDV GIVEQGKMRL SGRIKDTVIV HGVSYGIPEL ETYLQTVEGV
THSFLAAAPY RAPGQETEGF VVFYSPTFDL DSEDAPAKLF ATHRALRDVS VKLITLPPQQ
IIPIPINQME KTTLGKLSRA RLVNLLKQGE LAKHIDRAEE LVSIARGASF VAPSTETEKT
LAGIYAGIFN LSVSDMSASE NFFELGGTSI DVIRLKREGE SAFDLPEIPT IQILKHPVIS
SLAKYVDSLI SKDASQEEYD PIVPLQLTGN KTPIFMVHPG VGEVLIFVNL AKYFQNERPF
YALRARGFEP GHPFFTTMDE MVSCYAAAVK RTQPHGPYAI AGYSYGGVVA FEVAKRLEAM
GDEVKFTGLI NIPPNIADRM HEIDWTGGML NLSYFLGLVS KQDANDLAPS MRPLTRKEQL
EIVWKLSPPE RLVELQLTPE KLDHWVDIAG SLIECGKTYE PGSSVSVLDV FYAIPLRGSK
EDWLNKQLKP WAGYSRAEPS YTDVPGQHYT LMDFDHVPGF QKIFRSRLEA RGL
//
