RED1_COCH4
ID RED1_COCH4 Reviewed; 352 AA.
AC N4WR35; Q8NJQ2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=NADP-dependent oxidoreductase RED1 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305|PubMed:20192833};
DE AltName: Full=T-toxin biosynthesis protein RED1 {ECO:0000305};
GN Name=RED1 {ECO:0000303|PubMed:20192833}; ORFNames=COCC4DRAFT_45938;
OS Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665024;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=20192833; DOI=10.1094/mpmi-23-4-0458;
RA Inderbitzin P., Asvarak T., Turgeon B.G.;
RT "Six new genes required for production of T-toxin, a polyketide determinant
RT of high virulence of Cochliobolus heterostrophus to maize.";
RL Mol. Plant Microbe Interact. 23:458-472(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
RN [4]
RP FUNCTION.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=8953776; DOI=10.2307/3870419;
RA Yang G., Rose M.S., Turgeon B.G., Yoder O.C.;
RT "A polyketide synthase is required for fungal virulence and production of
RT the polyketide T-toxin.";
RL Plant Cell 8:2139-2150(1996).
RN [5]
RP FUNCTION.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=12236595; DOI=10.1094/mpmi.2002.15.9.883;
RA Rose M.S., Yun S.-H., Asvarak T., Lu S.-W., Yoder O.C., Turgeon B.G.;
RT "A decarboxylase encoded at the Cochliobolus heterostrophus translocation-
RT associated Tox1B locus is required for polyketide (T-toxin) biosynthesis
RT and high virulence on T-cytoplasm maize.";
RL Mol. Plant Microbe Interact. 15:883-893(2002).
RN [6]
RP FUNCTION.
RX PubMed=16529376; DOI=10.1094/mpmi-19-0139;
RA Baker S.E., Kroken S., Inderbitzin P., Asvarak T., Li B.Y., Shi L.,
RA Yoder O.C., Turgeon B.G.;
RT "Two polyketide synthase-encoding genes are required for biosynthesis of
RT the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus.";
RL Mol. Plant Microbe Interact. 19:139-149(2006).
CC -!- FUNCTION: NADP-dependent oxidoreductase; part of the Tox1B locus, one
CC of the 2 loci that mediate the biosynthesis of T-toxin, a family of
CC linear polyketides 37 to 45 carbons in length, of which the major
CC component is 41 carbons, and which leads to high virulence to maize
CC (PubMed:8953776, PubMed:20192833). One of the PKSs (PKS1 or PKS2) could
CC synthesize a precursor, used subsequently by the other PKS as starter
CC unit, to add additional carbons (PubMed:16529376). Variability in the
CC length of the final carbon backbone C35-47 could be achieved by varying
CC the number of condensation cycles, or use of different starter or
CC extender units or might be due to decarboxylation of the penultimate
CC product, catalyzed by DEC1 (PubMed:12236595). Additional proteins are
CC required for the biosynthesis of T-toxin, including oxidoreductases
CC RED1, RED2, RED3, LAM1 and OXI1, as well as esterase TOX9
CC (PubMed:20192833). {ECO:0000269|PubMed:12236595,
CC ECO:0000269|PubMed:16529376, ECO:0000269|PubMed:20192833,
CC ECO:0000269|PubMed:8953776}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192833}.
CC -!- DISRUPTION PHENOTYPE: Significantly reduces the production of T-toxin
CC and decreases the virulence to maize (PubMed:20192833).
CC {ECO:0000269|PubMed:20192833}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; AF525909; AAM88292.1; -; Genomic_DNA.
DR EMBL; KB733525; ENH98582.1; -; Genomic_DNA.
DR RefSeq; XP_014072492.1; XM_014217017.1.
DR AlphaFoldDB; N4WR35; -.
DR SMR; N4WR35; -.
DR EnsemblFungi; ENH98582; ENH98582; COCC4DRAFT_45938.
DR GeneID; 25845245; -.
DR HOGENOM; CLU_026673_29_1_1; -.
DR OrthoDB; 884151at2759; -.
DR PHI-base; PHI:2839; -.
DR Proteomes; UP000012338; Unassembled WGS sequence.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205; PTHR43205; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase.
FT CHAIN 1..352
FT /note="NADP-dependent oxidoreductase RED1"
FT /id="PRO_0000437647"
FT BINDING 166..169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT BINDING 285..287
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT CONFLICT 166
FT /note="G -> C (in Ref. 1; AAM88292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 38473 MW; 20C4705D94C6B055 CRC64;
MYQNKSLIFK NPPIGWPKPD VDFGVECRPI DINGDIPLGG VILKNCYVSL DPYQRGRMRA
PTVDSYSPPF TIGDPMEGHV ISRVIRSAST KLQPGDFVSG VGPIQEFSVL SAGVVDGFTR
IENPYNLNLE IFLGPLGMPG LTAYSSFYEI GKPKKGETIF ISAASGAVGQ LVGQLAKREG
LYVIGSVGDD EKVEFITKGL GFDVGFNYKK EVIGEALMRV APEGIDIYFD NVGGQTLESA
LYAMRPRGRI VVSGMISQYN LQPSELYGVK NLFMVITNRI TIQGFIVTDS DMGPKYSAEH
LKNVSQWIYD GSLKPKIHVD TGMDHACQSF INMLKGRKIG KAVLQIADLN GD
