OXI1_COCH4
ID OXI1_COCH4 Reviewed; 232 AA.
AC N4WE73; D2SZX7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Dehydrogenase OXI1 {ECO:0000305};
DE EC=1.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10001};
DE AltName: Full=T-toxin biosynthesis protein OXI1 {ECO:0000305};
DE Flags: Precursor;
GN Name=OXI1 {ECO:0000303|PubMed:23236275}; ORFNames=COCC4DRAFT_155491;
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 Tox1A 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; FJ943499; ADB23430.1; -; Genomic_DNA.
DR EMBL; KB733545; ENH98548.1; -; Genomic_DNA.
DR RefSeq; XP_014072458.1; XM_014216983.1.
DR AlphaFoldDB; N4WE73; -.
DR SMR; N4WE73; -.
DR EnsemblFungi; ENH98548; ENH98548; COCC4DRAFT_155491.
DR GeneID; 25839391; -.
DR HOGENOM; CLU_010194_1_3_1; -.
DR OrthoDB; 913128at2759; -.
DR PHI-base; PHI:2837; -.
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 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; NAD; Oxidoreductase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..232
FT /note="Dehydrogenase OXI1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000437645"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 232 AA; 24632 MW; C603FD41AA28D014 CRC64;
MTETFKVAIT FVSPSSEALA QSIIDSINKS ADTTRAIKIQ ADMRDTDSPL RIIDATICAF
GPNIDILVNN AGVESLVSLS ELGLQDFNEC IDVNFRAVVF MTKSVIPYLR SPGRIINISS
SSAHAGGLSS GIYAASKAAV EALARFWATS LGPQGHSVNT VVPGLTQTDM YERIIAEESS
AAYHRTVASM TPMGGRVGTP EDIARIVSLL VEPRSQWVTG QTISATGGLI LL
