STR7_STRTC
ID STR7_STRTC Reviewed; 336 AA.
AC A0A3B1EFQ1;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Aldo-keto reductase str7 {ECO:0000303|PubMed:30258052};
DE EC=1.1.1.- {ECO:0000305|PubMed:30258052};
DE AltName: Full=Strobilurin A biosynthesis cluster protein r7 {ECO:0000303|PubMed:30258052};
GN Name=str7 {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, 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: Aldo-keto reductase; part of the gene cluster that mediates
CC the biosynthesis of strobilurin A, an antifungal polyketide that
CC contains a key beta-methoxyacrylate toxophore that targets the complex
CC III of the mitochondrial electron transport chain (PubMed:30258052).
CC Strobilurin biosynthesis begins with construction of benzoyl CoA by
CC step-wise elimination of ammonia from phenylalanine by the
CC 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:0000305|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 aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; KY070339; ATV82117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B1EFQ1; -.
DR SMR; A0A3B1EFQ1; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..336
FT /note="Aldo-keto reductase str7"
FT /id="PRO_0000449344"
FT ACT_SITE 62
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 154..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 206..220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 283..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
SQ SEQUENCE 336 AA; 36832 MW; B0A15B31596AFDDF CRC64;
MPLPTRKIGQ SLVSEIGFGS MGIARLGPSG FYGVVESDDE RFKVLDAAHA AGCTFWDSAH
LYGDSEELIG KWLKRTGKRN DIFLATKFGI TPQGVRGDPD FVKEQCATSL ERLGVDCIDL
FYQHRVDPKT PIEITVGAMA ELVKEGKVKY LGLSECSAKA LRRAHAVHPI AALQIEYSPF
VLDIEDPKIA LLETARELGV TIVAYSPLGR GLLTGQYKSP DDFEPNDFRR TIPKFSADNF
PKILDVVAQL KKIGEKHNAT PGQVTLAWIL AQGPEFIVIP GTKKIKYLEE NVGAASIKLT
EEEVAAVRKL AEESEIPGDR NARMGAMLID SPELPQ
