RED2_COCH4
ID RED2_COCH4 Reviewed; 265 AA.
AC N4WE43; C3JXE8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Dehydrogenase RED2 {ECO:0000303|PubMed:16529376};
DE EC=1.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10001};
DE AltName: Full=T-toxin biosynthesis protein RED2 {ECO:0000305};
GN Name=RED2 {ECO:0000303|PubMed:20192833}; ORFNames=COCC4DRAFT_155544;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; ACP34152.1; -; Genomic_DNA.
DR EMBL; KB733569; ENH98523.1; -; Genomic_DNA.
DR RefSeq; XP_014072433.1; XM_014216958.1.
DR AlphaFoldDB; N4WE43; -.
DR SMR; N4WE43; -.
DR EnsemblFungi; ENH98523; ENH98523; COCC4DRAFT_155544.
DR GeneID; 25839400; -.
DR HOGENOM; CLU_010194_5_0_1; -.
DR OrthoDB; 1373099at2759; -.
DR PHI-base; PHI:2835; -.
DR Proteomes; UP000012338; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Glycoprotein; Membrane; NAD; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..265
FT /note="Dehydrogenase RED2"
FT /id="PRO_0000437643"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 265 AA; 29001 MW; 4598C1D75294BDD2 CRC64;
MWKIESFLLS KLFLCIALCT AYVAFSSAMM EPGLWLLSRP IVPLNRTSTV FGLTIVAIGL
SALSSWLSKL TLNNFTSDDS WDWSQEIVVV TGASSGIGAE IVRLLAELSI KTFILDPVPP
DNSVLKNGSV HYYKVDITKP KEVSAAAREI QVKFSSPTVL INNAGVGLAK NLLDENETER
RHLMNVNLLS QFTTVQEFLP AMIEKNHGHI VTMASSASYI SSPQIVSYAA SKAALVGFHE
GLGIELVKRY NAKKIRTTLV FAPLL
