ID   RED3_COCH4              Reviewed;         196 AA.
AC   N4WW42; C3JXE9;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Dehydrogenase RED3 {ECO:0000303|PubMed:16529376};
DE            EC=1.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10001};
DE   AltName: Full=T-toxin biosynthesis protein RED3 {ECO:0000305};
GN   Name=RED3 {ECO:0000303|PubMed:20192833}; ORFNames=COCC4DRAFT_155403;
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: Dehydrogenase; part of the Tox1B locus, one of the 2 loci
CC       that mediate the biosynthesis of T-toxin, a family of linear
CC       polyketides 37 to 45 carbons in length, of which the major component is
CC       41 carbons, and which leads to high virulence to maize (PubMed:8953776,
CC       PubMed:20192833). One of the PKSs (PKS1 or PKS2) could synthesize a
CC       precursor, used subsequently by the other PKS as starter unit, to add
CC       additional carbons (PubMed:16529376). Variability in the length of the
CC       final carbon backbone C35-47 could be achieved by varying the number of
CC       condensation cycles, or use of different starter or extender units or
CC       might be due to decarboxylation of the penultimate product, catalyzed
CC       by DEC1 (PubMed:12236595). Additional proteins are required for the
CC       biosynthesis of T-toxin, including oxidoreductases RED1, RED2, RED3,
CC       LAM1 and OXI1, as well as esterase TOX9 (PubMed:20192833).
CC       {ECO:0000269|PubMed:12236595, ECO:0000269|PubMed:16529376,
CC       ECO:0000269|PubMed:20192833, ECO:0000269|PubMed:8953776}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
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 short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF525909; ACP34153.1; -; Genomic_DNA.
DR   EMBL; KB733525; ENH98580.1; -; Genomic_DNA.
DR   RefSeq; XP_014072490.1; XM_014217015.1.
DR   AlphaFoldDB; N4WW42; -.
DR   SMR; N4WW42; -.
DR   EnsemblFungi; ENH98580; ENH98580; COCC4DRAFT_155403.
DR   GeneID; 25839374; -.
DR   HOGENOM; CLU_1390094_0_0_1; -.
DR   OrthoDB; 1373099at2759; -.
DR   PHI-base; PHI:2836; -.
DR   Proteomes; UP000012338; Unassembled WGS sequence.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..196
FT                   /note="Dehydrogenase RED3"
FT                   /id="PRO_0000437644"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   196 AA;  22273 MW;  C6480DE6FF2297A0 CRC64;
     MGLVKGNCGC YWGIKGHWSR NCSPVCEIAN KNYYSRRGIA PRRTFWSVSN KSLVHLDANS
     LMIDYENVFY YTTDITSNKA IIESSERIRQ DHGNPSVLIN NAGVANGKTI LEESEDERRR
     VFNVDILAHF SLVREFLPDM IKHNHGHIVT VASTASFLAR PQLVSYSCCK TALIAFHEGL
     SQELRMRHNA RKVRTT