ID   VRDA_ASPPA              Reviewed;         343 AA.
AC   B9WYE6;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Versiconal hemiacetal acetate reductase;
DE            EC=1.1.1.353;
DE   AltName: Full=VHA reductase;
GN   Name=vrdA;
OS   Aspergillus parasiticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 3-27 AND
RP   214-25, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 26691 / NRRL 2999 / CBS 921.70;
RX   PubMed=19211038; DOI=10.1016/j.fgb.2008.12.005;
RA   Shima Y., Shiina M., Shinozawa T., Ito Y., Nakajima H., Adachi Y., Yabe K.;
RT   "Participation in aflatoxin biosynthesis by a reductase enzyme encoded by
RT   vrdA gene outside the aflatoxin gene cluster.";
RL   Fungal Genet. Biol. 46:221-231(2009).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=16349333; DOI=10.1128/aem.60.7.2561-2567.1994;
RA   Matsushima K., Ando Y., Hamasaki T., Yabe K.;
RT   "Purification and characterization of two versiconal hemiacetal acetate
RT   reductases involved in aflatoxin biosynthesis.";
RL   Appl. Environ. Microbiol. 60:2561-2567(1994).
CC   -!- FUNCTION: Catalyzes 3 reactions: from hydroxyversicolorone (HVN) to
CC       versicolorone (VONE), from versiconal hemiacetal acetate (VHA) to
CC       versiconol acetate (VOAc) and from versiconal (VHOH) to versiconol
CC       (VOH). Probably not an aflatoxin biosynthesis gene: may be involved in
CC       the vertical branching steps connecting the main pathway from HVN to
CC       VHOH with the side pathway from VONE to VOH.
CC       {ECO:0000269|PubMed:19211038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-versicolorone + NADP(+) = 1'-hydroxyversicolorone + H(+)
CC         + NADPH; Xref=Rhea:RHEA:35691, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:73281, ChEBI:CHEBI:77907;
CC         EC=1.1.1.353; Evidence={ECO:0000269|PubMed:19211038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-versiconol acetate + NADP(+) = (2S,3S)-versiconal
CC         hemiacetal acetate + H(+) + NADPH; Xref=Rhea:RHEA:35695,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:72673, ChEBI:CHEBI:77975; EC=1.1.1.353;
CC         Evidence={ECO:0000269|PubMed:19211038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-versiconol + NADP(+) = (2S-3S)-versiconal hemiacetal +
CC         H(+) + NADPH; Xref=Rhea:RHEA:35699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77947,
CC         ChEBI:CHEBI:77950; EC=1.1.1.353;
CC         Evidence={ECO:0000269|PubMed:19211038};
CC   -!- DISRUPTION PHENOTYPE: Aflatoxin production is not inhibited, while the
CC       enzyme activity catalyzing the reaction from versiconal hemiacetal
CC       acetate (VHA), to versiconol acetate (VOAc), which branches from the
CC       main pathway, significantly decreases. {ECO:0000269|PubMed:19211038}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC       reductase 2 subfamily. {ECO:0000305}.
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DR   EMBL; AB025578; BAH24200.1; -; Genomic_DNA.
DR   EMBL; AB025579; BAH24201.1; -; mRNA.
DR   AlphaFoldDB; B9WYE6; -.
DR   SMR; B9WYE6; -.
DR   KEGG; ag:BAH24200; -.
DR   BRENDA; 1.1.1.353; 523.
DR   GO; GO:0102974; F:hydroxyversicolorone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102975; F:versiconal hemiacetal acetate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102976; F:versiconal reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   CHAIN           1..343
FT                   /note="Versiconal hemiacetal acetate reductase"
FT                   /id="PRO_0000424161"
FT   ACT_SITE        59
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..239
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            87
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  38698 MW;  32AA44AEE1DEDAA3 CRC64;
     MEYARLGDSG LKVSKVILGC MGYGSPEWQG WVLNEEESLP LIEHAYNKGI RTWDTADMYS
     HGKSEEIVGK ALKKYNIPRS RVVILTKCYF GVDDQGNFPS PLSTGRQNEG DYLNRVGLSR
     RHILEAVDAS VERLGTYIDV LQIHRLDRET PREEIMRALN DVVESGKARY IGASSMAAWE
     FQTLQNIAIR NGWHKFISMQ NYHNLIAREE EREMIPYCLD SGVSLIPWSP VARGALARPW
     ASRSTLRENT DAGISILVRA RESESDKAII DRVEELADKK GISMAQVAIA WSLSHPSEYP
     IVGLNTKDRI DEAVASVQVK LTPEEIQYLE EPYVPKAIHP GER