Detail Information for IndEnz0010001389
IED ID IndEnz0010001389
Enzyme Type ID esterase001389
Protein Name Dehydrogenase RED3
EC 1.1.1.1
T-toxin biosynthesis protein RED3
Gene Name RED3 COCC4DRAFT_155403
Organism Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern corn leaf blight fungus) (Bipolaris maydis)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Pleosporaceae Bipolaris Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris maydis) Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern corn leaf blight fungus) (Bipolaris maydis)
Enzyme Sequence MGLVKGNCGCYWGIKGHWSRNCSPVCEIANKNYYSRRGIAPRRTFWSVSNKSLVHLDANSLMIDYENVFYYTTDITSNKAIIESSERIRQDHGNPSVLINNAGVANGKTILEESEDERRRVFNVDILAHFSLVREFLPDMIKHNHGHIVTVASTASFLARPQLVSYSCCKTALIAFHEGLSQELRMRHNARKVRTT
Enzyme Length 196
Uniprot Accession Number N4WW42
Absorption
Active Site ACT_SITE 166; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10001
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10001}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
DNA Binding
EC Number 1.1.1.1
Enzyme Function FUNCTION: Dehydrogenase; part of the Tox1B locus, one of the 2 loci that mediate the biosynthesis of T-toxin, a family of linear polyketides 37 to 45 carbons in length, of which the major component is 41 carbons, and which leads to high virulence to maize (PubMed:8953776, PubMed:20192833). One of the PKSs (PKS1 or PKS2) could synthesize a precursor, used subsequently by the other PKS as starter unit, to add additional carbons (PubMed:16529376). Variability in the length of the final carbon backbone C35-47 could be achieved by varying the number of condensation cycles, or use of different starter or extender units or might be due to decarboxylation of the penultimate product, catalyzed by DEC1 (PubMed:12236595). Additional proteins are required for the biosynthesis of T-toxin, including oxidoreductases RED1, RED2, RED3, LAM1 and OXI1, as well as esterase TOX9 (PubMed:20192833). {ECO:0000269|PubMed:12236595, ECO:0000269|PubMed:16529376, ECO:0000269|PubMed:20192833, ECO:0000269|PubMed:8953776}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192833}.
nucleotide Binding
Features Active site (1); Chain (1)
Keywords NAD;Oxidoreductase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,273
Kinetics
Metal Binding
Rhea ID RHEA:10736; RHEA:10740
Cross Reference Brenda