ID   RPPA_STRC0              Reviewed;         377 AA.
AC   B0FYK7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=1,3,6,8-tetrahydroxynaphthalene synthase {ECO:0000303|PubMed:18612244};
DE            Short=THNS {ECO:0000303|PubMed:18612244};
DE            EC=2.3.1.233 {ECO:0000269|PubMed:18612244};
DE   AltName: Full=1,3,6,8-tetrahydroxynaphthalene synthesis polyketide synthase type III {ECO:0000305};
GN   Name=rppA {ECO:0000303|PubMed:18612244};
OS   Streptomyces peucetius subsp. caesius.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=55158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 27952 / DSM 41231 / NBRC 14660 / 106FI;
RX   PubMed=18612244;
RA   Ghimire G.P., Oh T.J., Liou K., Sohng J.K.;
RT   "Identification of a cryptic type III polyketide synthase (1,3,6,8-
RT   tetrahydroxynaphthalene synthase) from Streptomyces peucetius ATCC 27952.";
RL   Mol. Cells 26:362-367(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of melanin but also various
CC       secondary metabolites containing a naphthoquinone ring. Catalyzes the
CC       iterative condensation of five CoA-linked malonyl units to form a
CC       pentaketide intermediate. THNS subsequently catalyzes the dual
CC       intramolecular Claisen and aldol condensations of this linear
CC       intermediate to produce the fused ring of 1,3,6,8-
CC       tetrahydroxynaphthalene (THN). {ECO:0000269|PubMed:18612244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5 H(+) + 5 malonyl-CoA = 5 CO2 + 5 CoA + H2O + naphthalene-
CC         1,3,6,8-tetrol; Xref=Rhea:RHEA:41524, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18365,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384; EC=2.3.1.233;
CC         Evidence={ECO:0000269|PubMed:18612244};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC       {ECO:0000250|UniProtKB:Q54240}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FCA7}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; EU365174; ABY71276.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0FYK7; -.
DR   SMR; B0FYK7; -.
DR   KEGG; ag:ABY71276; -.
DR   BioCyc; MetaCyc:MON-18701; -.
DR   BRENDA; 2.3.1.233; 6073.
DR   UniPathway; UPA00785; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR   GO; GO:0042438; P:melanin biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR   InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR   InterPro; IPR011141; Polyketide_synthase_type-III.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11877; PTHR11877; 1.
DR   Pfam; PF02797; Chal_sti_synt_C; 1.
DR   Pfam; PF00195; Chal_sti_synt_N; 1.
DR   PIRSF; PIRSF000451; PKS_III; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Melanin biosynthesis; Transferase.
FT   CHAIN           1..377
FT                   /note="1,3,6,8-tetrahydroxynaphthalene synthase"
FT                   /id="PRO_0000430879"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250|UniProtKB:Q54240"
SQ   SEQUENCE   377 AA;  39081 MW;  B73728DE83D172A1 CRC64;
     MRVPVAVDDL VAPSTMGERH TVIDRGTSVA AVHTALPPHR YAQSDLTELI ADLCLEPGAD
     RALLRRLHTS AGVRTRHLAL PIEQYAGLGD FGQANAAWLT VGLALAEEAL SGALDAAGLT
     AADIDLLVCT SITGVAAPSL DARLAVRMGM RADVKRVPVF GLGCVGGAAG LGRLHDYLLG
     HPDDTAVLLS VELCSLTLQR DGSLANLVAG ALFGDGAAAV VARGGDAGRR GAGWPMVAAT
     RGHLYPDTEH LLGWRIGASG FRVVVDAGIP DVVRTHLGGD LRNFLATHGL VPDDIGTWIC
     HPGGPKVLAA VGDALELPDG ALDSSWRSLA GVGNLSSASV LRVLEDVATR CRPDPGTWGV
     LLAMGPGFCA EFVLLRW