STR9_STRTC
ID STR9_STRTC Reviewed; 463 AA.
AC A0A3B1EFQ2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=FAD-dependent monooxygenase str9 {ECO:0000303|PubMed:30258052};
DE EC=1.-.-.- {ECO:0000269|PubMed:30258052};
DE AltName: Full=Strobilurin A biosynthesis cluster protein r9 {ECO:0000303|PubMed:30258052};
GN Name=str9 {ECO:0000303|PubMed:30258052};
OS Strobilurus tenacellus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Physalacriaceae; Strobilurus.
OX NCBI_TaxID=41251;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND BIOTECHNOLOGY.
RC STRAIN=CBS 621.79;
RX PubMed=30258052; DOI=10.1038/s41467-018-06202-4;
RA Nofiani R., de Mattos-Shipley K., Lebe K.E., Han L.C., Iqbal Z.,
RA Bailey A.M., Willis C.L., Simpson T.J., Cox R.J.;
RT "Strobilurin biosynthesis in Basidiomycete fungi.";
RL Nat. Commun. 9:3940-3940(2018).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=563391; DOI=10.7164/antibiotics.30.806;
RA Anke T., Oberwinkler F., Steglich W., Schramm G.;
RT "The strobilurins--new antifungal antibiotics from the basidiomycete
RT Strobilurus tenacellus.";
RL J. Antibiot. 30:806-810(1977).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=6271595; DOI=10.1016/0014-5793(81)81190-8;
RA Becker W.F., von Jagow G., Anke T., Steglich W.;
RT "Oudemansin, strobilurin A, strobilurin B and myxothiazol: new inhibitors
RT of the bc1 segment of the respiratory chain with an E-beta-methoxyacrylate
RT system as common structural element.";
RL FEBS Lett. 132:329-333(1981).
RN [4]
RP REVIEW ON BIOTECHNOLOGY.
RX PubMed=29711574;
RX DOI=10.1002/(sici)1521-3773(19990517)38:10<1328::aid-anie1328>3.0.co;2-1;
RA Sauter H., Steglich W., Anke T.;
RT "Strobilurins: evolution of a new class of active substances.";
RL Angew. Chem. Int. Ed. 38:1328-1349(1999).
RN [5]
RP REVIEW ON BIOTECHNOLOGY.
RX PubMed=12146165; DOI=10.1002/ps.520;
RA Bartlett D.W., Clough J.M., Godwin J.R., Hall A.A., Hamer M.,
RA Parr-Dobrzanski B.;
RT "The strobilurin fungicides.";
RL Pest Manag. Sci. 58:649-662(2002).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of strobilurin A, an antifungal polyketide
CC that contains a key beta-methoxyacrylate toxophore that targets the
CC complex III of the mitochondrial electron transport chain
CC (PubMed:30258052). Strobilurin biosynthesis begins with construction of
CC benzoyl CoA by step-wise elimination of ammonia from phenylalanine by
CC the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-
CC Claisen reaction to form benzoic acid, which is activated to its CoA
CC thiolester benzoyl CoA by the dedicated CoA ligase str10
CC (PubMed:30258052). Benzoyl CoA forms the starter unit for the highly
CC reducing polyketide synthase stpks1 that produces the polyketide
CC prestrobilutin A (PubMed:30258052). The FAD-dependent oxygenase str9
CC then catalyzes the key oxidative rearrangement responsible for the
CC creation of the beta-methoxyacrylate toxophore (PubMed:30258052). Str9
CC performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by
CC Meinwald rearrangement to furnish the aldehyde intermediate (Probable).
CC Rapid enolization of the aldehyde intermediate would give the beta-
CC methoxyacrylate skeleton and methylations catalyzed by str2 and str3
CC complete the synthesis and lead to the peroduction of strobilurin A
CC (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase
CC str4 play a role in the shunt pathway leading to the production of
CC bolineol (PubMed:30258052). The cluster encodes no obvious halogenase
CC gene that could be involved in production of strobilurin B, nor any
CC obvious dimethylallyl-transferase that could be involved in the
CC production of strobilurin G (Probable). It is possible that unknown
CC proteins encoded in, or near, the cluster (such as str1 or stl1) may
CC form new classes of halogenases or dimethylally-transferases, or that
CC the responsible genes are located elsewhere on the genome (Probable).
CC Similarly, proteins encoded by str5/str6 hydrolases appear to have no
CC chemical role in the biosynthesis of strobilurin A (Probable). Finally,
CC no obvious self-resistance gene is found within the cluster (Probable).
CC {ECO:0000269|PubMed:30258052, ECO:0000305|PubMed:30258052}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30258052}.
CC -!- INDUCTION: Induced in strobilurin-producing conditions (on CGC medium
CC after 6 days of growth). {ECO:0000269|PubMed:30258052}.
CC -!- BIOTECHNOLOGY: The structure of strobilurin A was used for the
CC development of the major class of beta-methoxyacrylate agricultural
CC fungicides since its beta-methoxyacrylate toxophore targets the Qo site
CC of complex III of the mitochondrial electron transport chain and
CC prevents adenosine triphosphate synthesis (PubMed:563391,
CC PubMed:6271595). Compounds such as azoxystrobin (Syngenta) and Kresoxim
CC methyl (BASF) are among the most widely used fungicides worldwide
CC (PubMed:29711574, PubMed:12146165). This class of antifungals are used
CC as effective treatments against a broad range of destructive fungal
CC plant pathogens and make significant contributions to food security
CC (PubMed:29711574, PubMed:12146165). The strobilurin fungicides are
CC estimated to have been worth 3.4 billion dollars in 2015 and they make
CC up 25% of the fungicide market and 6.7% of the total crop protection
CC market (PubMed:30258052). {ECO:0000269|PubMed:563391,
CC ECO:0000269|PubMed:6271595, ECO:0000303|PubMed:12146165,
CC ECO:0000303|PubMed:29711574, ECO:0000303|PubMed:30258052}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; KY070339; ATV82119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B1EFQ2; -.
DR SMR; A0A3B1EFQ2; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; Oxidoreductase.
FT CHAIN 1..463
FT /note="FAD-dependent monooxygenase str9"
FT /id="PRO_0000449337"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 254..256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 344..348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 463 AA; 51392 MW; C627B78F0384E76C CRC64;
MAVDRKIRIA VVGGGPGGVI AALALSKSPN VEIDLYEAAT AFGDIGLSLG MPWRPWRILR
LLGLQGYLAA LLPPDQIPKE DVTVPTIHYR KSDQAVGEDI FTCTSLSGYT RFRRSHFHAA
LLPHLPSNCK TYTSKRLVSY AEPSNASDPI VITFADGTTA ECDVLVGADG IKSPTRASMY
NYAADEAEKA GRSAEANDLR SKIRAKFSGV EVYRSVISAE QLRAAAPDHH AFRCPTQFLG
KEKVRMPTYP IQSENSQFLN CALYICDYSR EGEDYPEPWV TDVEAKDLRS SLPDWEPEAQ
AAVSCMGEVV SRWAICTLSP LPFFQRSRVV LLGDAAVRVT TPFSTFSSDH CQTLACYDEL
PRCRLRPGDD AYILSEILTH PAVTRDNVQK ALEIYSEVRV PMSTHVLESS RRTGMDCALH
DEVAAADLKS LGERMQQEMV WAWEWNPEDE KKKALDLVEE RLV
