MLNS_PHANO
ID MLNS_PHANO Reviewed; 1785 AA.
AC A0A0A0RM07; Q0V687;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Mellein synthase {ECO:0000303|PubMed:25326302};
DE EC=2.3.1.- {ECO:0000269|PubMed:25326302};
DE AltName: Full=Polyketide synthase MLNS {ECO:0000305};
DE Short=PKS MLNS {ECO:0000305};
GN Name=MLNS {ECO:0000303|PubMed:25326302};
GN Synonyms=SN477 {ECO:0000303|PubMed:25326302}; ORFNames=SNOG_00477;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, FUNCTION, AND DOMAIN.
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=25326302; DOI=10.1128/aem.02745-14;
RA Chooi Y.H., Krill C., Barrow R.A., Chen S., Trengove R., Oliver R.P.,
RA Solomon P.S.;
RT "An in planta-expressed polyketide synthase produces (R)-mellein in the
RT wheat pathogen Parastagonospora nodorum.";
RL Appl. Environ. Microbiol. 81:177-186(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Polyketide synthase that produces (R)-mellein, a secondary
CC metabolite that inhibits the germination of wheat (Triticum aestivum)
CC and barrel medic (Medicago truncatula) seeds (PubMed:25326302).
CC Condensates 1 acetate starter unit and 4 extender malonate units
CC (PubMed:25326302). The nascent pentaketide intermediate then undergoes
CC an aldol cyclization and is aromatized via dehydration
CC (PubMed:25326302). The (R)-O-methylmellein isolated from P.nodorum is
CC most likely to be derived from (R)-mellein via an additional
CC methylation at the hydroxyl group. Interestingly, no O-
CC methyltransferase gene is encoded in the vicinity of MLNS on the
CC chromosome. Thus, the O-methylation is likely to be catalyzed by an
CC endogenous O-methyltransferase encoded elsewhere in the genome of
CC P.nodorum (PubMed:25326302). {ECO:0000269|PubMed:25326302}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25326302}.
CC -!- INDUCTION: Expression is highly induced during plant infection.
CC {ECO:0000269|PubMed:25326302}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydrogenase (DH)
CC domain that reduces hydroxyl groups to enoyl groups, a beta-
CC ketoreductase domain (KR) that reduces beta-ketone groups to hydroxyl
CC groups; and an acyl-carrier protein (ACP) that serves as the tether of
CC the growing and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:25326302}.
CC -!- DISRUPTION PHENOTYPE: Does not induce any observable growth defect but
CC impairs the production of both mellein and O-methylmellein.
CC {ECO:0000269|PubMed:25326302}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT91972.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KM365454; AIW00670.1; -; Genomic_DNA.
DR EMBL; CH445325; EAT91972.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001791162.1; XM_001791110.1.
DR AlphaFoldDB; A0A0A0RM07; -.
DR SMR; A0A0A0RM07; -.
DR STRING; 13684.SNOT_00477; -.
DR GeneID; 5967957; -.
DR KEGG; pno:SNOG_00477; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_35_3_1; -.
DR OrthoDB; 19161at2759; -.
DR PHI-base; PHI:3324; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1785
FT /note="Mellein synthase"
FT /id="PRO_0000447725"
FT DOMAIN 1706..1781
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:25326302"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..467
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25326302"
FT REGION 575..888
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25326302"
FT REGION 935..1203
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25326302"
FT REGION 1418..1608
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25326302"
FT REGION 1681..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 661
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1741
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1785 AA; 193492 MW; B9E5FFD73F70CF56 CRC64;
MATPDDPATP ALSLSASNSS SPTAASSVPP PTGTSEIQYD DVAIIGMSCR TAGGNDSPEK
LWRFIMDKKD ASGESPSWRW EPWVRRDTRN AKVIEKTISK GYFIEDLENF DASFFGISPK
EAEQMDPHQR LGLEVTWEAL EDAGINPQSL SGSDTAVYVG VDSDDYSRLL LEDIPNIEAW
MGIGTTAHGI PNRISYHLDL MGPSAAVDAA CASSMVAVHT GRQAILAGES RIAIVGGVNV
CLSPALFHML GAAGALSPDG VCLSFDEEAR GYARGEGAAI LILKKMSHAI MDGDHILATI
KGSAIAQDGK TNGIMAPNAK AQELVARKAL KQAGINALTV GYIEAHATST PLGDPTEVSA
ISAVYGVGRP TDTPALIGSI KPNVGHLEAA AGAISLVKAV MAVQKGIVPP QTRLNKLNTR
VDWAKSGLHV VRESTQWGTE DSPRRAAICS YGYGGTVSHA IIEQFAHAAD PFTASTSDDN
HPTLLLLSAP QGKQRLPAQS AALAEWISPA GAHESLRSIA ATLATRRAHH ENRAAFIVSS
HTEAAETLNL FSKGAEHDSI VQSRTLDNNI NKQIVWVFSG HGSHWSGMGK QLLQNAVFYR
TVAPLDIVVV QELGYSAIEA LKTGRFESSG QVQVLTYMTQ IGLIQLLKAK GVHPHAVIGH
SVGEIAASVA AGCLTPEEGM IIVTRRARLF AKVIGCGGMF LVSLPFAEVL AELGGRTDIV
AAIDSSPSSC VISGLNAPLE EYVEKLKNRG IRVFQVKTDI AFHSPMLEVL SKPLKESLEG
SLNPQPPNIK LYSTSQADTR HPARRDAEYW VDNMVKPVWL RPAVTAAIED HYRIFMEVST
HPIVSHSLDE TLAENGASDF TTIHTMKKEQ SAEKCILHAV AQLWTKGVKI DFKFLGRQWS
REVPKIRWSH KRFWKEVSTG SASAQTVHDP DKNNMLGQRM VVAGTNMTIF TTALDESSKP
FPMPHQLHGT DIIPVSVYVN TFIKATGGKV LSKMELRVPL AVTNDVRNVQ VIVDGQSVKV
ASRLSSSDDM SWVTHSTASW ENEPSANVLP SLDVSSVIKR IGTRVSETFS VDYLKKTGVS
GMAFPWAVND HYNNTKEMLV TLDNDPEHET MSWDPCSWGA TLDAATSVGA TLFSREVKLR
IVSHIDRLTI YSSDPPPKRY HLYVTEASSS QVHACSADIS VLDLSGTLLA RIESIRFTEV
EATPTKSTSI ESGVHQIAWV PARLSEKPLS LEQIVLVSED DAKLEQYANE LQRQAPKIVK
LTSAAKLRDN GALFMREKNA TVIYCPGTVT SLEDVASASH RFIWEVATAI KFLVENSISA
KFFVILDRTF LAGSPTALAQ GALYGLARVV ASEHSDIWGG LIDNEGPLFP VMPLKYVQDQ
DITRYIDGVP RVARMRPFTK QQRYAPSTAR TLLPKPEGTY VLTGGLGALG LETCDFLIEK
GARRIVVISR RDIPARSQWS KASENLAPIL ERVKAMEKTG ASIYFVSLDI GAADAHQQLL
FALERLSLPP VLGVIHASGV LEDSLLVDTT SDSFARVLSP KISGALALHK AFPPGTLDFF
VLYSSIGQLV GTSGQSSYAA GNSFLDVLAA HRRSQGDNAI AFQWTAWRGL GMATSTDFLT
LELQSKGITD VGRDEAFQAW EHMSKYDVDQ AVVTRTLALE ADDILPCALL EEVVVRKARA
QDQSAPASGN ASDSSGRPTA SADLKPWLDV KIRECVALVM GVEDIEEIDT RVPLSDYGVD
SIMTIALRQK LQSKLKIKVP QTLMWNYPTV SAMVGWFQKQ FEEGQ
