RDT1_ELSFA
ID RDT1_ELSFA Reviewed; 267 AA.
AC B0ZT44;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Elsinochrome reductase 1 {ECO:0000303|PubMed:18957608};
DE EC=1.1.1.- {ECO:0000305|PubMed:18957608};
DE AltName: Full=Elsinochromes biosynthesis cluster protein RDT1 {ECO:0000303|PubMed:18957608};
GN Name=RDT1 {ECO:0000303|PubMed:18957608};
OS Elsinoe fawcettii (Citrus scab fungus) (Sphaceloma fawcettii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40997;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND INDUCTION.
RX PubMed=18957608; DOI=10.1099/mic.0.2008/019414-0;
RA Chung K.R., Liao H.L.;
RT "Determination of a transcriptional regulator-like gene involved in
RT biosynthesis of elsinochrome phytotoxin by the citrus scab fungus, Elsinoe
RT fawcettii.";
RL Microbiology 154:3556-3566(2008).
RN [2]
RP REVIEW.
RX PubMed=21199563; DOI=10.1111/j.1364-3703.2010.00663.x;
RA Chung K.R.;
RT "Elsinoe fawcettii and Elsinoe australis: the fungal pathogens causing
RT citrus scab.";
RL Mol. Plant Pathol. 12:123-135(2011).
CC -!- FUNCTION: Reductase; part of the gene cluster that mediates the
CC biosynthesis of elsinochromes, pigments consisting of at least four
CC interconvertible tautomers (A, B, C and D) that have a core phenolic
CC quinone to which various side chains are attached and which play an
CC important role in fungal pathogenesis (PubMed:18957608). The non-
CC reducing polyketide synthase PKS1 was proposed to iteratively catalyze
CC decarboxylation between acetyl-CoA and malonyl-CoA subunits for
CC polyketide chain elongation. The released polyketide undergoes
CC cyclization to form an aromatic ring, and proceeds via serial
CC modification steps to produce the heptaketide back- bone of
CC elsinochrome. As elsinochrome has a symmetrical structure, two
CC identical heptaketides are fused to form a core 1,2-dihydrobenzo-
CC perylene ring structure, which can then be successively modified to
CC produce the various derivatives of elsinochrome. Some of these
CC reactions may be cooperatively carried out, at least in part, by the
CC products of RDT1, OXR1 and PKS1. PRF1, embedded within the elsinochrome
CC cluster possibly functions to stabilize some of the biosynthetic
CC enzymes required for elsinochrome production. As prefoldin is a hexamer
CC containing 2 a and 4 b subunits, additional prefoldin subunits, whose
CC coding genes may not immediately link to the elsinochrome biosynthetic
CC gene cluster, are required to fulfill the chaperone function. In
CC addition, no methyltransferase-coding gene exists within the
CC biosynthetic gene cluster, even though elsinochrome has four methyl
CC groups at positions C3, C7, C8 and C12. Apparently, the identified gene
CC cluster does not contain the entire entourage of genes responsible for
CC elsinochrome biosynthesis. Once elsinochrome is synthesized, it must be
CC exported outside the fungal cells, which is probably accomplished by
CC the ECT1 transporter, to avoid toxicity (PubMed:21199563).
CC {ECO:0000269|PubMed:18957608, ECO:0000303|PubMed:21199563}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor TSF1 (PubMed:18957608). Expression is induced by
CC the presence of the cluster-specific polyketide synthase PKS1
CC (PubMed:18957608). Expression is up-regulated during nitrogen
CC starvation (PubMed:18957608). {ECO:0000269|PubMed:18957608}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU401704; ABZ01830.1; -; Genomic_DNA.
DR AlphaFoldDB; B0ZT44; -.
DR SMR; B0ZT44; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..267
FT /note="Elsinochrome reductase 1"
FT /id="PRO_0000445822"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 18..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 45..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 71..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 163..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 196..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 267 AA; 28170 MW; 53AD8B5F18AAF416 CRC64;
MSALQALSTS RLDGKVALVT GSGRGIGAAI ATELANRGAS VVVNYANSPD AAQTVVDAIK
KNGGDAIALQ ADVSDVKQTI KLFDDAVAHY GQLDIAVSNS GVVSFGHLKD VTEEEFDRVF
AINTRGQFFV AREAYKHLSV GGRIILMGSI TGQAKGVPKH TVYSGTKGAI ETFVRCMAID
CGDKRITVNC VAPGGIKTDM YHAVCKEYIP NGENLTNEQV DEYAATWSPL NRVGQPIDVA
RVCGFLASQD GEWINGKVLG IDGAACM
