AF121_ALTAL
ID AF121_ALTAL Reviewed; 297 AA.
AC Q50LG0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Oxidoreductase AFT12-1 {ECO:0000303|Ref.1};
DE EC=1.-.-.- {ECO:0000305|Ref.1};
DE AltName: Full=AF-toxin biosynthesis protein 12-1 {ECO:0000303|Ref.1};
GN Name=AFT12-1 {ECO:0000303|Ref.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=NAF8;
RX DOI=10.1007/s10327-004-0170-3;
RA Ruswandi S., Kitani K., Akimitsu K., Tsuge T., Shiraishi T., Yamamoto M.;
RT "Structural analysis of cosmid clone pcAFT-2 carrying AFT10-1 encoding an
RT acyl-CoA dehydrogenase involved in AF-toxin production in the strawberry
RT pathotype of Alternaria alternata.";
RL J. Gen. Plant Pathol. 71:107-116(2005).
RN [2]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=12019223; DOI=10.1093/genetics/161.1.59;
RA Hatta R., Ito K., Hosaki Y., Tanaka T., Tanaka A., Yamamoto M.,
RA Akimitsu K., Tsuge T.;
RT "A conditionally dispensable chromosome controls host-specific
RT pathogenicity in the fungal plant pathogen Alternaria alternata.";
RL Genetics 161:59-70(2002).
RN [3]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT "Dissection of the host range of the fungal plant pathogen Alternaria
RT alternata by modification of secondary metabolism.";
RL Mol. Microbiol. 52:399-411(2004).
RN [4]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=18986255; DOI=10.1094/mpmi-21-12-1591;
RA Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA Gomi K., Peever T.L., Akimitsu K.;
RT "Functional analysis of a multicopy host-selective ACT-toxin biosynthesis
RT gene in the tangerine pathotype of Alternaria alternata using RNA
RT silencing.";
RL Mol. Plant Microbe Interact. 21:1591-1599(2008).
RN [5]
RP REVIEW ON HOST-SELECTIVE TOXINS.
RX PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA Egusa M., Yamamoto M., Otani H.;
RT "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT alternata.";
RL FEMS Microbiol. Rev. 37:44-66(2013).
CC -!- FUNCTION: Oxidoreductase; part of the gene clusters that mediate the
CC biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible
CC for Alternaria black spot of strawberry disease by the strawberry
CC pathotype (Ref.1). AF-toxin I and III are valine derivatives of 2,3-
CC dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively,
CC while AF II is an isoleucine derivative of 2-hydroxy-valeric acid
CC (PubMed:15066029, Ref.1, PubMed:22846083). These derivatives are bound
CC to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) moiety
CC (PubMed:15066029, Ref.1, PubMed:22846083). On cellular level, AF-toxins
CC affect plasma membrane of susceptible cells and cause a sudden increase
CC in loss of K(+) after a few minutes of toxin treatment
CC (PubMed:22846083). The aldo-keto reductase AFTS1 catalyzes the
CC conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric
CC acid (2-HIV) by reduction of its ketone to an alcohol
CC (PubMed:15066029). The acyl-CoA ligase AFT1, the hydrolase AFT2 and the
CC enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase
CC AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450
CC monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in
CC the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural
CC moiety (PubMed:12019223, Ref.1, PubMed:18986255). The exact function of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have still to be determined (PubMed:12019223, Ref.1,
CC PubMed:18986255). {ECO:0000269|PubMed:12019223,
CC ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:18986255,
CC ECO:0000269|Ref.1, ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|Ref.1}.
CC -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC localized on conditionally dispensable chromosomes (CDCs), also called
CC supernumerary chromosomes, where they are present in multiple copies
CC (PubMed:12019223). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:12019223).
CC {ECO:0000269|PubMed:12019223}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; AB179766; BAD97697.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50LG0; -.
DR SMR; Q50LG0; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Virulence.
FT CHAIN 1..297
FT /note="Oxidoreductase AFT12-1"
FT /id="PRO_0000444869"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 14..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ SEQUENCE 297 AA; 32894 MW; BE4402C7C854E79A CRC64;
MVVHSLGSTN LQENQSAVGA IAAWRLQHAG YSRVTTLCRS NYDAVKTSGF RLSTSLWGKH
IYKPDRVAND IREVKHTEFD YVVDATKNIS ATWTLSISEI RQVVRPRTTI LSLQNGMQPE
RRFTKAFPAN TVLAGICFLS CSQISPGCIL QTSHIRPHAF YIGMSSSPSF RDAKQKLRRL
VSLDSSFLAV RDIRIQQWIK LITNVTFNSA TALMNAHTRD VLDSASGIEL VRALAEECYE
LGLALGMAIP QGTVDSIIED FLSAPPVVTS MLQDLRAGRP LELDALLGKL KTYLVIL
