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Norsolorinic acid ketoreductase (EC 1.1.1.349) (Aflatoxin biosynthesis ketoreductase nor-1) (Aflatoxin biosynthesis protein D) (Short chain dehydrogenase aflD)

 AFLD_ASPPU              Reviewed;         271 AA.
Q00278; A0A0F0I0S7; Q6UEH1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 69.
RecName: Full=Norsolorinic acid ketoreductase {ECO:0000303|PubMed:10584035};
EC=1.1.1.349 {ECO:0000269|PubMed:10584035};
AltName: Full=Aflatoxin biosynthesis ketoreductase nor-1 {ECO:0000305};
AltName: Full=Aflatoxin biosynthesis protein D {ECO:0000303|PubMed:15006741};
AltName: Full=Short chain dehydrogenase aflD {ECO:0000305};
Name=aflD {ECO:0000303|PubMed:15006741};
Synonyms=nor-1 {ECO:0000303|PubMed:7993094}; ORFNames=P875_00052988;
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 /
SU-1).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=1403190;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=7993094;
Trail F., Chang P.-K., Cary J., Linz J.E.;
"Structural and functional analysis of the nor-1 gene involved in the
biosynthesis of aflatoxins by Aspergillus parasiticus.";
Appl. Environ. Microbiol. 60:4078-4085(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=15094053; DOI=10.1016/S0014-5793(04)00327-8;
Yu J., Bhatnagar D., Cleveland T.E.;
"Completed sequence of aflatoxin pathway gene cluster in Aspergillus
parasiticus.";
FEBS Lett. 564:126-130(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
Nierman W.C.;
"Draft genome sequence of Aspergillus parasiticus SU-1.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=1339261;
Skory C.D., Chang P.K., Cary J., Linz J.E.;
"Isolation and characterization of a gene from Aspergillus parasiticus
associated with the conversion of versicolorin A to sterigmatocystin
in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 58:3527-3537(1992).
[5]
FUNCTION.
PubMed=8434913;
Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
Ullah A.H.J.;
"Purification of a 40-kilodalton methyltransferase active in the
aflatoxin biosynthetic pathway.";
Appl. Environ. Microbiol. 59:479-484(1993).
[6]
FUNCTION.
PubMed=8368836;
Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: conversion of
norsolorinic acid to averufin.";
Appl. Environ. Microbiol. 59:2486-2492(1993).
[7]
FUNCTION.
PubMed=8368837;
Yabe K., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: cyclase reaction in
the conversion of versiconal to versicolorin B and racemization of
versiconal hemiacetal acetate.";
Appl. Environ. Microbiol. 59:2493-2500(1993).
[8]
FUNCTION.
PubMed=10543813;
Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
"Cloning and characterization of the O-methyltransferase I gene (dmtA)
from Aspergillus parasiticus associated with the conversions of
demethylsterigmatocystin to sterigmatocystin and
dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 65:4987-4994(1999).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10584035;
Zhou R., Linz J.E.;
"Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
Aspergillus parasiticus.";
Appl. Environ. Microbiol. 65:5639-5641(1999).
[10]
FUNCTION.
PubMed=11055914; DOI=10.1128/AEM.66.11.4715-4719.2000;
Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G.,
Bhatnagar D., Cleveland T.E.;
"adhA in Aspergillus parasiticus is involved in conversion of 5'-
hydroxyaverantin to averufin.";
Appl. Environ. Microbiol. 66:4715-4719(2000).
[11]
FUNCTION.
PubMed=16256699; DOI=10.1006/bioo.2001.1216;
Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
Townsend C.A.;
"Hexanoate synthase, a specialized type I fatty acid synthase in
aflatoxin B1 biosynthesis.";
Bioorg. Chem. 29:293-307(2001).
[12]
FUNCTION.
PubMed=11996570; DOI=10.1021/ja012185v;
Udwary D.W., Casillas L.K., Townsend C.A.;
"Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
cytochrome P-450 in the final step of aflatoxin biosynthesis.";
J. Am. Chem. Soc. 124:5294-5303(2002).
[13]
REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
PubMed=15006741; DOI=10.1128/AEM.70.3.1253-1262.2004;
Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D.,
Cleveland T.E., Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
"Clustered pathway genes in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 70:1253-1262(2004).
[14]
FUNCTION.
PubMed=15528514; DOI=10.1128/AEM.70.11.6518-6524.2004;
Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
"Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
formation.";
Appl. Environ. Microbiol. 70:6518-6524(2004).
[15]
SUBCELLULAR LOCATION.
PubMed=14722624; DOI=10.1007/s00203-003-0643-3;
Lee L.W., Chiou C.H., Klomparens K.L., Cary J.W., Linz J.E.;
"Subcellular localization of aflatoxin biosynthetic enzymes Nor-1,
Ver-1, and OmtA in time-dependent fractionated colonies of Aspergillus
parasiticus.";
Arch. Microbiol. 181:204-214(2004).
[16]
INDUCTION.
PubMed=15054098; DOI=10.1074/jbc.M400075200;
Roze L.V., Miller M.J., Rarick M., Mahanti N., Linz J.E.;
"A novel cAMP-response element, CRE1, modulates expression of nor-1 in
Aspergillus parasiticus.";
J. Biol. Chem. 279:27428-27439(2004).
[17]
INDUCTION.
PubMed=15746358; DOI=10.1128/AEM.71.3.1539-1545.2005;
Miller M.J., Roze L.V., Trail F., Linz J.E.;
"Role of cis-acting sites NorL, a TATA box, and AflR1 in nor-1
transcriptional activation in Aspergillus parasiticus.";
Appl. Environ. Microbiol. 71:1539-1545(2005).
[18]
FUNCTION.
PubMed=15932995; DOI=10.1128/AEM.71.6.2999-3006.2005;
Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K.,
Nakajima H.;
"Aspergillus parasiticus cyclase catalyzes two dehydration steps in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 71:2999-3006(2005).
[19]
FUNCTION.
PubMed=16332900; DOI=10.1128/AEM.71.12.8963-8965.2005;
Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
"An aflatoxin biosynthesis cluster gene encodes a novel oxidase
required for conversion of versicolorin a to sterigmatocystin.";
Appl. Environ. Microbiol. 71:8963-8965(2005).
[20]
FUNCTION.
PubMed=15771506; DOI=10.1021/ja0455188;
Henry K.M., Townsend C.A.;
"Ordering the reductive and cytochrome P450 oxidative steps in
demethylsterigmatocystin formation yields general insights into the
biosynthesis of aflatoxin and related fungal metabolites.";
J. Am. Chem. Soc. 127:3724-3733(2005).
[21]
FUNCTION.
PubMed=16461654; DOI=10.1128/AEM.72.2.1096-1101.2006;
Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
"The aflatoxin biosynthesis cluster gene, aflX, encodes an
oxidoreductase involved in conversion of versicolorin A to
demethylsterigmatocystin.";
Appl. Environ. Microbiol. 72:1096-1101(2006).
[22]
FUNCTION.
PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y.,
Adachi Y., Nakajima H., Yabe K.;
"Involvement of the nadA gene in formation of G-group aflatoxins in
Aspergillus parasiticus.";
Fungal Genet. Biol. 45:1081-1093(2008).
[23]
FUNCTION.
PubMed=18403714; DOI=10.1126/science.1154711;
Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L.,
Kelleher N.L., Townsend C.A.;
"Deconstruction of iterative multidomain polyketide synthase
function.";
Science 320:243-246(2008).
[24]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19217941; DOI=10.1016/j.mycres.2009.01.013;
Hong S.Y., Linz J.E.;
"Functional expression and sub-cellular localization of the early
aflatoxin pathway enzyme Nor-1 in Aspergillus parasiticus.";
Mycol. Res. 113:591-601(2009).
[25]
DISRUPTION PHENOTYPE.
PubMed=22069731; DOI=10.3390/toxins3060647;
Abdel-Hadi A.M., Caley D.P., Carter D.R., Magan N.;
"Control of aflatoxin production of Aspergillus flavus and Aspergillus
parasiticus using RNA silencing technology by targeting aflD (nor-1)
gene.";
Toxins 3:647-659(2011).
[26]
INDUCTION.
PubMed=23113196;
Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
"Effect of curcumin on Aspergillus parasiticus growth and expression
of major genes involved in the early and late stages of aflatoxin
biosynthesis.";
Iran. J. Public Health 41:72-79(2012).
[27]
INDUCTION.
PubMed=24294264; DOI=10.1590/S1517-83822013000200045;
Yahyaraeyat R., Khosravi A.R., Shahbazzadeh D., Khalaj V.;
"The potential effects of Zataria multiflora Boiss essential oil on
growth, aflatoxin production and transcription of aflatoxin
biosynthesis pathway genes of toxigenic Aspergillus parasiticus.";
Braz. J. Microbiol. 44:643-649(2013).
[28]
INDUCTION.
PubMed=26217023; DOI=10.3382/ps/pev207;
Yin H.B., Chen C.H., Kollanoor-Johny A., Darre M.J.,
Venkitanarayanan K.;
"Controlling Aspergillus flavus and Aspergillus parasiticus growth and
aflatoxin production in poultry feed using carvacrol and trans-
cinnamaldehyde.";
Poult. Sci. 94:2183-2190(2015).
-!- FUNCTION: Norsolorinic acid ketoreductase; part of the gene
cluster that mediates the biosynthesis of aflatoxins, a group of
polyketide-derived furanocoumarins, and part of the most toxic and
carcinogenic compounds among the known mycotoxins (PubMed:7993094,
PubMed:15006741). The four major aflatoxins produced by
A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2),
aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The
first step of the pathway is the conversion of acetate to
norsolorinic acid (NOR) and requires the fatty acid synthase
subunits aflA and aflB, as well as the PKS aflC (PubMed:15006741).
AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender
units to synthesize the precursor NOR (PubMed:18403714). The
hexanoyl starter unit is provided to the acyl-carrier protein
(ACP) domain by the fungal fatty acid synthase aflA/aflB
(PubMed:16256699). The second step is the conversion of NOR to
averantin (AVN) and requires the norsolorinic acid ketoreductase
aflD, which catalyzes the dehydration of norsolorinic acid to form
(1'S)-averantin (PubMed:10584035, PubMed:19217941). The
norsolorinic acid reductases aflE and aflF may also play a role in
the conversion of NOR to AVN (PubMed:15006741). The cytochrome
P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to
5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is
performed by the 5'-hydroxyaverantin dehydrogenase aflH that
transforms HAVN to 5'-oxoaverantin (OAVN) which is further
converted to averufin (AVF) by aflK that plays a dual role in the
pathway, as a 5'-oxoaverantin cyclase that mediates conversion of
5'-oxoaverantin, as well as a versicolorin B synthase in a later
step in the pathway (PubMed:15006741, PubMed:11055914,
PubMed:15932995). The averufin oxidase aflI catalyzes the
conversion of AVF to versiconal hemiacetal acetate (VHA)
(PubMed:15006741). VHA is then the substrate for the versiconal
hemiacetal acetate esterase aflJ to yield versiconal (VAL)
(PubMed:15006741). Versicolorin B synthase aflK then converts VAL
to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin
which is required for DNA-binding, thus giving to aflatoxin its
activity as a mutagen (PubMed:15006741, PubMed:8368837,
PubMed:15932995). Then, the activity of the versicolorin B
desaturase aflL leads to versicolorin A (VERA) (PubMed:15006741,
PubMed:8368837). A branch point starts from VERB since it can also
be converted to dihydrodemethylsterigmatocystin (DMDHST), probably
also by aflL, VERA being a precursor for aflatoxins B1 and G1, and
DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next, the
versicolorin reductase aflM and the cytochrome P450 monooxygenase
aflN are involved in conversion of VERA to
demethylsterigmatocystin (DMST) (PubMed:15006741, PubMed:1339261,
PubMed:15771506). AflX and aflY seem also involved in this step,
through probable aflX-mediated epoxide ring-opening step following
versicolorin A oxidation and aflY-mediated Baeyer-Villiger
oxidation required for the formation of the xanthone ring
(PubMed:16332900, PubMed:16461654). The methyltransferase aflO
then leads to the modification of DMST to sterigmatocystin (ST),
and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813).
Both ST and DHST are then substrates of the O-methyltransferase
aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-
methylsterigmatocystin (DHOMST), respectively (PubMed:8434913).
Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to
aflatoxins B2 and G2, via the action of several enzymes including
O-methylsterigmatocystin oxidoreductase aflQ, the cytodhrome P450
monooxygenase aflU, but also the NADH-dependent flavin
oxidoreductase nadA which is specifically required for the
synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
ECO:0000269|PubMed:10584035, ECO:0000269|PubMed:11055914,
ECO:0000269|PubMed:11996570, ECO:0000269|PubMed:1339261,
ECO:0000269|PubMed:15528514, ECO:0000269|PubMed:15771506,
ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:16256699,
ECO:0000269|PubMed:16332900, ECO:0000269|PubMed:16461654,
ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
ECO:0000269|PubMed:19217941, ECO:0000269|PubMed:7993094,
ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
ECO:0000269|PubMed:8434913, ECO:0000305|PubMed:15006741}.
-!- CATALYTIC ACTIVITY: (1'S)-averantin + NADP(+) = norsolorinic acid
+ NADPH. {ECO:0000269|PubMed:10584035}.
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000269|PubMed:15094053, ECO:0000305|PubMed:15006741}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:14722624, ECO:0000269|PubMed:19217941}.
Vacuole {ECO:0000269|PubMed:19217941}.
-!- INDUCTION: Expression is stimulated by gluscoe (PubMed:15054098).
The promoter contains a CRE1 element (5'-TGACATAA-3') required for
cAMP-mediated stimulation of expression (PubMed:15054098).
Expression is also positively regulated by the cluster-specific
transcription factor aflR that binds to an AFLR1 element (5'-
TCGGCCAGCGA-3') (PubMed:15054098, PubMed:15746358). The promoter
contains also an aflD-specific element called NorL (residues -210
to -238) and required for full transcription (PubMed:15746358).
Natural plant compounds carvacrol (CR) and trans-cinnamaldehyde
(TC) strongly reduce the expession (PubMed:26217023). Zataria
multiflora essential oil reduces gene expression
(PubMed:24294264). Expression is also repressed by curcumin
(PubMed:23113196). {ECO:0000269|PubMed:15054098,
ECO:0000269|PubMed:15746358, ECO:0000269|PubMed:23113196,
ECO:0000269|PubMed:24294264, ECO:0000269|PubMed:26217023}.
-!- DISRUPTION PHENOTYPE: Leads to accumulation of norsolorinic acid
and a substantial reduced production of aflatoxin AFB1
(PubMed:7993094). {ECO:0000269|PubMed:7993094}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=KJK60791.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; L27801; AAA58798.1; -; Genomic_DNA.
EMBL; AY371490; AAS66005.1; -; Genomic_DNA.
EMBL; JZEE01000728; KJK60791.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; Q00278; -.
EnsemblFungi; KJK60791; KJK60791; P875_00052988.
KEGG; ag:AAA58798; -.
KO; K17644; -.
BRENDA; 1.1.1.349; 523.
BRENDA; 1.1.1.B25; 523.
UniPathway; UPA00287; -.
Proteomes; UP000033540; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; NADP; Oxidoreductase;
Reference proteome; Vacuole.
CHAIN 1 271 Norsolorinic acid ketoreductase.
/FTId=PRO_0000054736.
NP_BIND 33 35 NADP. {ECO:0000250|UniProtKB:Q6PQJ9}.
NP_BIND 57 58 NADP. {ECO:0000250|UniProtKB:Q6PQJ9}.
ACT_SITE 185 185 {ECO:0000250|UniProtKB:Q6PQJ9}.
BINDING 164 164 NADP; via amide nitrogen.
{ECO:0000250|UniProtKB:Q6PQJ9}.
SEQUENCE 271 AA; 29569 MW; 34059A857672059A CRC64;
MNGSLSQHDQ ERLSTPYRDG PPEETVYLVT GASRGIGRGL IEAFLQRPKS TVVAWLRNVR
TATPALSALT VAEGSRMIIV QLNSDSETDA QAAVQTLREE HGVTHLDVVV ANAAMATNFG
PASTMPLEHL QAHMMVNMYA PVLLFQATRL MLQQSKQQAK FVLIGAPIST ITNMHDYSRA
PLTAYGVSKL AANYMVRKFH FENKWLTAFI IDPGHVQTDM GDQGARLMGR PQAPTTVADS
VAGICARIDE ATKETTSGHF VIHTDGSQLP W


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EIAAB05618 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,Cbr,Cbr1,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandi
EIAAB08641 CGI-92,Coenzyme Q biosynthesis protein 4 homolog,COQ4,Homo sapiens,Human,Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
EIAAB08639 Coenzyme Q biosynthesis protein 4 homolog,Coq4,Rat,Rattus norvegicus,Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
EIAAB08640 Coenzyme Q biosynthesis protein 4 homolog,Coq4,Mouse,Mus musculus,Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial


 

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