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AFLI_ASPPU
ID   AFLI_ASPPU              Reviewed;         285 AA.
AC   Q12437; Q6UEF9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Averufin oxidase A {ECO:0000305|PubMed:7793957};
DE            EC=1.-.-.- {ECO:0000305|PubMed:10806361};
DE   AltName: Full=Aflatoxin biosynthesis protein I {ECO:0000303|PubMed:15006741};
GN   Name=aflI {ECO:0000303|PubMed:15006741};
GN   Synonyms=avfA {ECO:0000303|PubMed:10806361},
GN   ord-2 {ECO:0000303|PubMed:7793957};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PATHWAY.
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX   PubMed=7793957; DOI=10.1128/aem.61.6.2365-2371.1995;
RA   Yu J., Chang P.-K., Cary J.W., Wright M., Bhatnagar D., Cleveland T.E.,
RA   Payne G.A., Linz J.E.;
RT   "Comparative mapping of aflatoxin pathway gene clusters in Aspergillus
RT   parasiticus and Aspergillus flavus.";
RL   Appl. Environ. Microbiol. 61:2365-2371(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX   PubMed=10806361; DOI=10.1016/s0378-1119(00)00126-8;
RA   Yu J., Woloshuk C.P., Bhatnagar D., Cleveland T.E.;
RT   "Cloning and characterization of avfA and omtB genes involved in aflatoxin
RT   biosynthesis in three Aspergillus species.";
RL   Gene 248:157-167(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=1339261; DOI=10.1128/aem.58.11.3527-3537.1992;
RA   Skory C.D., Chang P.K., Cary J., Linz J.E.;
RT   "Isolation and characterization of a gene from Aspergillus parasiticus
RT   associated with the conversion of versicolorin A to sterigmatocystin in
RT   aflatoxin biosynthesis.";
RL   Appl. Environ. Microbiol. 58:3527-3537(1992).
RN   [5]
RP   FUNCTION.
RX   PubMed=8434913; DOI=10.1128/aem.59.2.479-484.1993;
RA   Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
RA   Ullah A.H.J.;
RT   "Purification of a 40-kilodalton methyltransferase active in the aflatoxin
RT   biosynthetic pathway.";
RL   Appl. Environ. Microbiol. 59:479-484(1993).
RN   [6]
RP   FUNCTION.
RX   PubMed=8368836; DOI=10.1128/aem.59.8.2486-2492.1993;
RA   Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
RT   "Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic
RT   acid to averufin.";
RL   Appl. Environ. Microbiol. 59:2486-2492(1993).
RN   [7]
RP   FUNCTION.
RX   PubMed=8368837; DOI=10.1128/aem.59.8.2493-2500.1993;
RA   Yabe K., Hamasaki T.;
RT   "Stereochemistry during aflatoxin biosynthesis: cyclase reaction in the
RT   conversion of versiconal to versicolorin B and racemization of versiconal
RT   hemiacetal acetate.";
RL   Appl. Environ. Microbiol. 59:2493-2500(1993).
RN   [8]
RP   FUNCTION.
RX   PubMed=10543813; DOI=10.1128/aem.65.11.4987-4994.1999;
RA   Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
RT   "Cloning and characterization of the O-methyltransferase I gene (dmtA) from
RT   Aspergillus parasiticus associated with the conversions of
RT   demethylsterigmatocystin to sterigmatocystin and
RT   dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in aflatoxin
RT   biosynthesis.";
RL   Appl. Environ. Microbiol. 65:4987-4994(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=10584035; DOI=10.1128/aem.65.12.5639-5641.1999;
RA   Zhou R., Linz J.E.;
RT   "Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
RT   Aspergillus parasiticus.";
RL   Appl. Environ. Microbiol. 65:5639-5641(1999).
RN   [10]
RP   FUNCTION.
RX   PubMed=11055914; DOI=10.1128/aem.66.11.4715-4719.2000;
RA   Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G., Bhatnagar D.,
RA   Cleveland T.E.;
RT   "adhA in Aspergillus parasiticus is involved in conversion of 5'-
RT   hydroxyaverantin to averufin.";
RL   Appl. Environ. Microbiol. 66:4715-4719(2000).
RN   [11]
RP   FUNCTION.
RX   PubMed=16256699; DOI=10.1006/bioo.2001.1216;
RA   Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
RA   Townsend C.A.;
RT   "Hexanoate synthase, a specialized type I fatty acid synthase in aflatoxin
RT   B1 biosynthesis.";
RL   Bioorg. Chem. 29:293-307(2001).
RN   [12]
RP   FUNCTION.
RX   PubMed=11996570; DOI=10.1021/ja012185v;
RA   Udwary D.W., Casillas L.K., Townsend C.A.;
RT   "Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
RT   cytochrome P-450 in the final step of aflatoxin biosynthesis.";
RL   J. Am. Chem. Soc. 124:5294-5303(2002).
RN   [13]
RP   REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
RX   PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA   Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA   Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT   "Clustered pathway genes in aflatoxin biosynthesis.";
RL   Appl. Environ. Microbiol. 70:1253-1262(2004).
RN   [14]
RP   FUNCTION.
RX   PubMed=15528514; DOI=10.1128/aem.70.11.6518-6524.2004;
RA   Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
RT   "Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
RT   formation.";
RL   Appl. Environ. Microbiol. 70:6518-6524(2004).
RN   [15]
RP   FUNCTION.
RX   PubMed=15932995; DOI=10.1128/aem.71.6.2999-3006.2005;
RA   Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K., Nakajima H.;
RT   "Aspergillus parasiticus cyclase catalyzes two dehydration steps in
RT   aflatoxin biosynthesis.";
RL   Appl. Environ. Microbiol. 71:2999-3006(2005).
RN   [16]
RP   FUNCTION.
RX   PubMed=16332900; DOI=10.1128/aem.71.12.8963-8965.2005;
RA   Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
RT   "An aflatoxin biosynthesis cluster gene encodes a novel oxidase required
RT   for conversion of versicolorin a to sterigmatocystin.";
RL   Appl. Environ. Microbiol. 71:8963-8965(2005).
RN   [17]
RP   FUNCTION.
RX   PubMed=15771506; DOI=10.1021/ja0455188;
RA   Henry K.M., Townsend C.A.;
RT   "Ordering the reductive and cytochrome P450 oxidative steps in
RT   demethylsterigmatocystin formation yields general insights into the
RT   biosynthesis of aflatoxin and related fungal metabolites.";
RL   J. Am. Chem. Soc. 127:3724-3733(2005).
RN   [18]
RP   FUNCTION.
RX   PubMed=16461654; DOI=10.1128/aem.72.2.1096-1101.2006;
RA   Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
RT   "The aflatoxin biosynthesis cluster gene, aflX, encodes an oxidoreductase
RT   involved in conversion of versicolorin A to demethylsterigmatocystin.";
RL   Appl. Environ. Microbiol. 72:1096-1101(2006).
RN   [19]
RP   FUNCTION.
RX   PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
RA   Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y., Adachi Y.,
RA   Nakajima H., Yabe K.;
RT   "Involvement of the nadA gene in formation of G-group aflatoxins in
RT   Aspergillus parasiticus.";
RL   Fungal Genet. Biol. 45:1081-1093(2008).
RN   [20]
RP   FUNCTION.
RX   PubMed=18403714; DOI=10.1126/science.1154711;
RA   Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L., Kelleher N.L.,
RA   Townsend C.A.;
RT   "Deconstruction of iterative multidomain polyketide synthase function.";
RL   Science 320:243-246(2008).
CC   -!- FUNCTION: Averufin oxidase; part of the gene cluster that mediates the
CC       biosynthesis of aflatoxins, a group of polyketide-derived
CC       furanocoumarins, and part of the most toxic and carcinogenic compounds
CC       among the known mycotoxins (PubMed:15006741). The four major aflatoxins
CC       produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2),
CC       aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The
CC       first step of the pathway is the conversion of acetate to norsolorinic
CC       acid (NOR) and requires the fatty acid synthase subunits aflA and aflB,
CC       as well as the PKS aflC (PubMed:15006741). AflC combines a hexanoyl
CC       starter unit and 7 malonyl-CoA extender units to synthesize the
CC       precursor NOR (PubMed:18403714). The hexanoyl starter unit is provided
CC       to the acyl-carrier protein (ACP) domain by the fungal fatty acid
CC       synthase aflA/aflB (PubMed:16256699). The second step is the conversion
CC       of NOR to averantin (AVN) and requires the norsolorinic acid
CC       ketoreductase aflD, which catalyzes the dehydration of norsolorinic
CC       acid to form (1'S)-averantin (PubMed:10584035). The norsolorinic acid
CC       reductases aflE and aflF may also play a role in the conversion of NOR
CC       to AVN (PubMed:15006741). The cytochrome P450 monooxygenase aflG then
CC       catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN)
CC       (PubMed:8368836). The next step is performed by the 5'-hydroxyaverantin
CC       dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which
CC       is further converted to averufin (AVF) by aflK that plays a dual role
CC       in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion
CC       of 5'-oxoaverantin, as well as a versicolorin B synthase in a later
CC       step in the pathway (PubMed:15006741, PubMed:11055914,
CC       PubMed:15932995). The averufin oxidase aflI catalyzes the conversion of
CC       AVF to versiconal hemiacetal acetate (VHA) (PubMed:10806361,
CC       PubMed:15006741). VHA is then the substrate for the versiconal
CC       hemiacetal acetate esterase aflJ to yield versiconal (VAL)
CC       (PubMed:15006741). Versicolorin B synthase aflK then converts VAL to
CC       versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which
CC       is required for DNA-binding, thus giving to aflatoxin its activity as a
CC       mutagen (PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the
CC       activity of the versicolorin B desaturase aflL leads to versicolorin A
CC       (VERA) (PubMed:15006741, PubMed:8368837). A branch point starts from
CC       VERB since it can also be converted to dihydrodemethylsterigmatocystin
CC       (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins
CC       B1 and G1, and DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next,
CC       the versicolorin reductase aflM and the cytochrome P450 monooxygenase
CC       aflN are involved in conversion of VERA to demethylsterigmatocystin
CC       (DMST) (PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and
CC       aflY seem also involved in this step, through probable aflX-mediated
CC       epoxide ring-opening step following versicolorin A oxidation and aflY-
CC       mediated Baeyer-Villiger oxidation required for the formation of the
CC       xanthone ring (PubMed:16332900, PubMed:16461654). The methyltransferase
CC       aflO then leads to the modification of DMST to sterigmatocystin (ST),
CC       and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both
CC       ST and DHST are then substrates of the O-methyltransferase aflP to
CC       yield O-methylsterigmatocystin (OMST) and dihydro-O-
CC       methylsterigmatocystin (DHOMST), respectively (PubMed:8434913). Finally
CC       OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2
CC       and G2, via the action of several enzymes including O-
CC       methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450
CC       monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase
CC       nadA which is specifically required for the synthesis of AFG1
CC       (PubMed:15006741, PubMed:11996570, PubMed:15528514, PubMed:18486503).
CC       {ECO:0000269|PubMed:10543813, ECO:0000269|PubMed:10584035,
CC       ECO:0000269|PubMed:10806361, ECO:0000269|PubMed:11055914,
CC       ECO:0000269|PubMed:11996570, ECO:0000269|PubMed:1339261,
CC       ECO:0000269|PubMed:15528514, ECO:0000269|PubMed:15771506,
CC       ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:16256699,
CC       ECO:0000269|PubMed:16332900, ECO:0000269|PubMed:16461654,
CC       ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
CC       ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
CC       ECO:0000269|PubMed:8434913, ECO:0000305|PubMed:15006741}.
CC   -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC       {ECO:0000305|PubMed:15006741, ECO:0000305|PubMed:7793957}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the avfA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA87599.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA97502.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L41150; AAA87599.1; ALT_FRAME; mRNA.
DR   EMBL; L40840; AAA97502.1; ALT_FRAME; mRNA.
DR   EMBL; AY371490; AAS66010.1; -; Genomic_DNA.
DR   EMBL; JZEE01000729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q12437; -.
DR   UniPathway; UPA00287; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:GO_Central.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..285
FT                   /note="Averufin oxidase A"
FT                   /id="PRO_0000058077"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        25
FT                   /note="S -> G (in Ref. 1; AAA87599/AAA97502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="R -> T (in Ref. 1; AAA87599/AAA97502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="P -> S (in Ref. 1; AAA87599/AAA97502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="Q -> H (in Ref. 1; AAA87599/AAA97502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="Q -> H (in Ref. 1; AAA87599/AAA97502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="A -> G (in Ref. 1; AAA87599/AAA97502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  30933 MW;  7AB1E6EF4349FB4E CRC64;
     MVTYALLGAT GATGSSILRH LLQKSPDSLH IQVLVRSKVK LLQAFPDLET TRRPQVHVIQ
     GMSTDSDALS ECLRNASIVF MCVAQNGSPI GTTLCQDSAR PIISVLQQQQ QSEGASYQPC
     TIVQLRSASL NPALAAQVPA FVHRIVSFCL FANYADIKQA CQYYSEAQKQ GTLEYILVDP
     PTLHDANGTH PTGYRLISTE PQATALSYAD LGAAMCEIAH RESEFHGRAV GVTATGRVRQ
     TWGVLLRHLL EGGSSRLRET IAKEAVVVRV LCIFLVILAC LMSSL
 
 
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