DTXS3_METRA
ID DTXS3_METRA Reviewed; 370 AA.
AC E9FCP6;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Aldo-keto reductase dtxS3 {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305|PubMed:22232661};
DE AltName: Full=Destruxin synthesis protein 3 {ECO:0000303|PubMed:22232661};
GN Name=dtxS3 {ECO:0000303|PubMed:22232661}; ORFNames=MAA_10045;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22232661; DOI=10.1073/pnas.1115983109;
RA Wang B., Kang Q., Lu Y., Bai L., Wang C.;
RT "Unveiling the biosynthetic puzzle of destruxins in Metarhizium species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:1287-1292(2012).
CC -!- FUNCTION: Aldo-keto reductase; part of the gene cluster that mediates
CC the biosynthesis of destruxins, insecticidal cyclic hexadepsipeptides
CC which induce flaccid paralysis and visceral muscle contraction in
CC insects through targeting the calcium channels and vacuolar-type
CC ATPases (PubMed:22232661). The aldo-keto reductase dtxS3 converts
CC alpha-ketoisocaproic acid from deaminated leucine into alpha-
CC hydroxyisocaproic acid (HIC), which is the first substrate for
CC destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate
CC decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last
CC substrate for the destruxin assembly line performed by dtxS1
CC (PubMed:22232661). The nonribosomal peptide synthetase dtxS1
CC synthesizes destruxins B and B2, whereas the cytochrome P450
CC monooxygenase dtxS2 is required to convert destruxin B into other
CC destruxin derivatives, including destructins C, D, A and E
CC (PubMed:22232661). Destruxin E-diol (ED) is further produced in a non-
CC enzymatic manner from destruxin E (PubMed:22232661). Destruxins play an
CC important role in virulence and escape from insect host immune defenses
CC (PubMed:22232661). {ECO:0000269|PubMed:22232661}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22232661}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of destruxins
CC (PubMed:22232661). {ECO:0000269|PubMed:22232661}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; ADNJ02000010; EFY94502.2; -; Genomic_DNA.
DR RefSeq; XP_007826234.2; XM_007828043.2.
DR AlphaFoldDB; E9FCP6; -.
DR SMR; E9FCP6; -.
DR EnsemblFungi; EFY94502; EFY94502; MAA_10045.
DR GeneID; 19264331; -.
DR KEGG; maj:MAA_10045; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase.
FT CHAIN 1..370
FT /note="Aldo-keto reductase dtxS3"
FT /id="PRO_0000436438"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 204..205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 259..269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 333..341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
SQ SEQUENCE 370 AA; 41982 MW; 3E99E4BE6EBDCC65 CRC64;
MAKVSLEKLL RIPPSLTQSI SQTKVDYLNL GHSGLRVSRP ILGGLHLGSR KWLPWVLDEE
KALPILKAAY DLGVNTWDTA NVYSNGESER IIAKALSKYK IPRNKVVLMT KCYRVMSDPE
RFDPGSGVTM HHELADYSKD YVNQWGLSRR ALFSAVEASL DRLNTSYIDV LQIHRFDHTV
PPEETMSALN DLIRAGMVRY IGASSMWTFQ FATLQHIAET KGLTKFISMQ NHYNLIYREE
EREMNQYCKM TGVGLIPWGP LASGRLARRP TQEEGSLRAS CSAHGSLYES DDYNVDRIIQ
RVAEIAEKRG WPMSHVSLAW LNRRVTAPII GFGSVGRIEE ALAARGKELS RDEEQYLEEL
YVPQRIQGHS
