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Dehydrogenase OXI1 (EC 1.1.1.1) (T-toxin biosynthesis protein OXI1)

 OXI1_COCH4              Reviewed;         232 AA.
N4WE73; D2SZX7;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 1.
05-DEC-2018, entry version 23.
RecName: Full=Dehydrogenase OXI1 {ECO:0000305};
EC=1.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10001};
AltName: Full=T-toxin biosynthesis protein OXI1 {ECO:0000305};
Flags: Precursor;
Name=OXI1 {ECO:0000303|PubMed:23236275}; ORFNames=COCC4DRAFT_155491;
Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T)
(Southern corn leaf blight fungus) (Bipolaris maydis).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
Pleosporaceae; Bipolaris.
NCBI_TaxID=665024;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=C4 / ATCC 48331 / race T;
PubMed=20192833; DOI=10.1094/MPMI-23-4-0458;
Inderbitzin P., Asvarak T., Turgeon B.G.;
"Six new genes required for production of T-toxin, a polyketide
determinant of high virulence of Cochliobolus heterostrophus to
maize.";
Mol. Plant Microbe Interact. 23:458-472(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C4 / ATCC 48331 / race T;
PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
"Diverse lifestyles and strategies of plant pathogenesis encoded in
the genomes of eighteen Dothideomycetes fungi.";
PLoS Pathog. 8:E1003037-E1003037(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C4 / ATCC 48331 / race T;
PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
Grigoriev I.V., Zhong S., Turgeon B.G.;
"Comparative genome structure, secondary metabolite, and effector
coding capacity across Cochliobolus pathogens.";
PLoS Genet. 9:E1003233-E1003233(2013).
[4]
FUNCTION.
STRAIN=C4 / ATCC 48331 / race T;
PubMed=8953776; DOI=10.1105/tpc.8.11.2139;
Yang G., Rose M.S., Turgeon B.G., Yoder O.C.;
"A polyketide synthase is required for fungal virulence and production
of the polyketide T-toxin.";
Plant Cell 8:2139-2150(1996).
[5]
FUNCTION.
STRAIN=C4 / ATCC 48331 / race T;
PubMed=12236595; DOI=10.1094/MPMI.2002.15.9.883;
Rose M.S., Yun S.-H., Asvarak T., Lu S.-W., Yoder O.C., Turgeon B.G.;
"A decarboxylase encoded at the Cochliobolus heterostrophus
translocation-associated Tox1B locus is required for polyketide (T-
toxin) biosynthesis and high virulence on T-cytoplasm maize.";
Mol. Plant Microbe Interact. 15:883-893(2002).
[6]
FUNCTION.
PubMed=16529376; DOI=10.1094/MPMI-19-0139;
Baker S.E., Kroken S., Inderbitzin P., Asvarak T., Li B.Y., Shi L.,
Yoder O.C., Turgeon B.G.;
"Two polyketide synthase-encoding genes are required for biosynthesis
of the polyketide virulence factor, T-toxin, by Cochliobolus
heterostrophus.";
Mol. Plant Microbe Interact. 19:139-149(2006).
-!- FUNCTION: Dehydrogenase; part of the Tox1A 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}.
-!- 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};
-!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192833}.
-!- DISRUPTION PHENOTYPE: Significantly reduces the production of T-
toxin and decreases the virulence to maize (PubMed:20192833).
{ECO:0000269|PubMed:20192833}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; FJ943499; ADB23430.1; -; Genomic_DNA.
EMBL; KB733545; ENH98548.1; -; Genomic_DNA.
RefSeq; XP_014072458.1; XM_014216983.1.
ProteinModelPortal; N4WE73; -.
SMR; N4WE73; -.
EnsemblFungi; ENH98548; ENH98548; COCC4DRAFT_155491.
GeneID; 25839391; -.
OrthoDB; EOG092C3TSH; -.
Proteomes; UP000012338; Unassembled WGS sequence.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
3: Inferred from homology;
Complete proteome; Glycoprotein; NAD; Oxidoreductase; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 232 Dehydrogenase OXI1. {ECO:0000255}.
/FTId=PRO_0000437645.
ACT_SITE 133 133 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 42 42 NADP. {ECO:0000250|UniProtKB:P16544}.
BINDING 137 137 NADP. {ECO:0000250|UniProtKB:P16544}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
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


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