ID   NPS3_SERL9              Reviewed;         962 AA.
AC   F8P1W3;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Atromentin synthetase nps3;
DE            EC=2.3.1.-;
DE   AltName: Full=Nonribosomal peptide synthase-like enzyme 3;
DE            Short=NRPS-like;
GN   Name=nps3; ORFNames=SERLADRAFT_416588;
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S7.9;
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=27699944; DOI=10.1111/1462-2920.13558;
RA   Tauber J.P., Schroeckh V., Shelest E., Brakhage A.A., Hoffmeister D.;
RT   "Bacteria induce pigment formation in the basidiomycete Serpula
RT   lacrymans.";
RL   Environ. Microbiol. 18:5218-5227(2016).
CC   -!- FUNCTION: An L-tyrosine:2-oxoglutarate aminotransferase (probably amt1)
CC       and atromentin synthetase nps3 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 nps3 adenylation (A) domain, covalent
CC       tethering of the monomers as a thioester and oxoester onto the nps3
CC       thiolation (T) and thioesterase (TE) domains, respectively, and
CC       symmetric C-C-bond formation between two monomers catalyzed by the nps3
CC       TE domain leads to atromentin. Follow-up products of atromentin in
CC       S.lacrymans include atromentic acid, xerocomic acid, isoxerocomic acid
CC       and variegatic acid. {ECO:0000269|PubMed:27699944}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:27699944}.
CC   -!- INDUCTION: Up-regulated upon coincubation of the fungus with the
CC       terrestrial bacteria Streptomyces iranensis, Bacillus subtilis or
CC       Pseudomonas putida. {ECO:0000269|PubMed:27699944}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; GL945436; EGO23141.1; -; Genomic_DNA.
DR   RefSeq; XP_007320381.1; XM_007320319.1.
DR   AlphaFoldDB; F8P1W3; -.
DR   SMR; F8P1W3; -.
DR   EnsemblFungi; EGO23141; EGO23141; SERLADRAFT_416588.
DR   GeneID; 18813499; -.
DR   KEGG; sla:SERLADRAFT_416588; -.
DR   HOGENOM; CLU_000022_23_6_1; -.
DR   InParanoid; F8P1W3; -.
DR   Proteomes; UP000008064; Unassembled WGS sequence.
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: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; IPR020806; PKS_PP-bd.
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; SM00823; PKS_PP; 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..962
FT                   /note="Atromentin synthetase nps3"
FT                   /id="PRO_0000442626"
FT   DOMAIN          601..679
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          55..469
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          606..676
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          702..805
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         638
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   962 AA;  106043 MW;  33C9800B83047FD1 CRC64;
     MAPAPTSVPL VSQPNVISDL KTALAVQGSA SDHPRTLHQL LSQAAERYPL QQLGFISSSA
     HDSSIQTKSY STFNQHVRNL ARALTDWKKP VGSIVVVYLT EHEDNMAAVW ACLLAGYIPC
     LQPALSAQQS HKEGHINHIK NLFLSATWLT NEIGAEQVMS VDGIDIHLFS DLKLAAEGYN
     VPADWAAVEA KPDDEAILFL TSGSTGFSKA VVHTHRTIIA SCYAKGQSYG LTSETNVLNW
     VGFDHVAGSL EMHITPLLFG SYQLHVHAST ILSDPLSFLR LIDDKSINIA FAPNFLLAKL
     ARDLEKRSEL YGAFDLSSVK RINSGGEAVV SKTAKIFVTV LKALAKDPSK VSFVVSAGFG
     MTETCAGCIY DPIDLSVINP MHEFLDLGRP IQGCEMRIVD PEDGITLRPD GESGELQVRG
     PMVFARYYNN PQATSSSFVE GRWYRTGDIG IIEKGVMRLS GRIKDTVIVH GVSYGIPELE
     TYLQLVEGVT HSFLAAAPYR APGQETEGFV VFYSPTFDLN EEDASNKLAA THRALRDISV
     KMITLPPQQI IPIPIDQMEK TTLGKLSRAR LLTLFKQGEL AKHIARADEL LSEARGATFV
     VPATITETAF AKIFAGVFNL STDDISAADN FFELGGTSID VIRLKREGET VFGLPEIPII
     QILKHPVLRD LAKYIDALVS KDNTQQEYDP IVPLQLTGNK TPIFFVHPGV GEVLIFVNLA
     KYFQNERPFY AFRARGFEPG QPFFSKMDEM VSSYAAAMKR TQPKGPYAIA GYSYGGVIAF
     EVAKRLEAGG DEVKFVGLIN IPPHIADRMH EIDWTGGMLN LSYFLGLVSK QDADDLAPTL
     RPLTRKEQLD VVWKLSPPER LVELQLTPEK LDHWVDIAGS LIECGKDYNP SGSVAVADVF
     YAIPLRGSKS DWLNNQLKPW SGFSRTEPAF TDVPGRHYTL MDFDHVPQFQ KIFRSRLEAR
     GV