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AFLV_ASPPU
ID   AFLV_ASPPU              Reviewed;         508 AA.
AC   Q6UEF4; A0A0F0I2B1;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Cytochrome P450 monooxygenase aflV {ECO:0000303|PubMed:15006741};
DE            EC=1.-.-.- {ECO:0000305|PubMed:15006741};
DE   AltName: Full=Aflatoxin biosynthesis protein V {ECO:0000303|PubMed:15006741};
GN   Name=aflV {ECO:0000303|PubMed:15006741};
GN   Synonyms=cypX {ECO:0000303|PubMed:10855719}; ORFNames=P875_00052993;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX   PubMed=10855719; DOI=10.1007/s002530051660;
RA   Yu J., Chang P.-K., Bhatnagar D., Cleveland T.E.;
RT   "Genes encoding cytochrome P450 and monooxygenase enzymes define one end of
RT   the aflatoxin pathway gene cluster in Aspergillus parasiticus.";
RL   Appl. Microbiol. Biotechnol. 53:583-590(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND NOMENCLATURE.
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX   PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA   Yu J., Bhatnagar D., Cleveland T.E.;
RT   "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT   parasiticus.";
RL   FEBS Lett. 564:126-130(2004).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the 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:15006741). VHA is
CC       then the substrate for the versiconal hemiacetal acetate esterase aflJ
CC       to yield versiconal (VAL) (PubMed:15006741). Versicolorin B synthase
CC       aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC       ring of aflatoxin which is required for DNA-binding, thus giving to
CC       aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837,
CC       PubMed:15932995). Then, the activity of the versicolorin B desaturase
CC       aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837).
CC       A branch point starts from VERB since it can also be converted to
CC       dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA
CC       being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins
CC       B2 and G2 (PubMed:15006741). Next, the versicolorin reductase aflM and
CC       the cytochrome P450 monooxygenase aflN are involved in conversion of
CC       VERA to demethylsterigmatocystin (DMST) (PubMed:15006741,
CC       PubMed:1339261, PubMed:15771506). AflX and aflY seem also involved in
CC       this step, through probable aflX-mediated epoxide ring-opening step
CC       following versicolorin A oxidation and aflY-mediated Baeyer-Villiger
CC       oxidation required for the formation of the xanthone ring
CC       (PubMed:16332900, PubMed:16461654). The methyltransferase aflO then
CC       leads to the modification of DMST to sterigmatocystin (ST), and of
CC       DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both ST and
CC       DHST are then substrates of the O-methyltransferase aflP to yield O-
CC       methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin
CC       (DHOMST), respectively (PubMed:8434913). Finally OMST is converted to
CC       aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the
CC       action of several enzymes including O-methylsterigmatocystin
CC       oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also
CC       the NADH-dependent flavin oxidoreductase nadA which is specifically
CC       required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
CC       PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
CC       ECO:0000269|PubMed:10584035, 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC       {ECO:0000305|PubMed:15006741, ECO:0000305|PubMed:15094053}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY371490; AAS66022.1; -; Genomic_DNA.
DR   EMBL; JZEE01000729; KJK60772.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6UEF4; -.
DR   SMR; Q6UEF4; -.
DR   EnsemblFungi; KJK60772; KJK60772; P875_00052993.
DR   BioCyc; MetaCyc:MON-14034; -.
DR   UniPathway; UPA00287; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0045122; P:aflatoxin biosynthetic process; TAS:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..508
FT                   /note="Cytochrome P450 monooxygenase aflV"
FT                   /id="PRO_0000438342"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         453
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   508 AA;  56332 MW;  E02625B8436EB9B2 CRC64;
     MTNTAPRELI RAIEHVPLTW WFLAVGGAWI VSKIIKILQT AYFSPLRKIP GPWYARLTSA
     RLAWASFANN RIYYVQSLHD KYGSIVLIGP EEVDIADPVA AKQIHRMGSG FVKAPFYKLL
     SPGPVDNIFN FRDAKLHSTR RKLYAKGFTL NSLRQQWEPT IRNIVALTVE RIRHDAQQGE
     AEILGWWTLM ANETVCKLTF NGGHDTVRNG TKDPFVLMLE RRMGDLAHLL QHFAPPLYYL
     GRLLGRAVPR LHDVFFSQET MFEAGKHVVA IARSARDAEG DRNLFVKALA AGDLESKIGG
     LNDTEIITDA GALLLAGSDP TALSLTYLIW CVLNRPKLQA ELESEVAGLQ GDITDAACAD
     LPILNAVIYE SLRLYGPAPG AMPRSPPPDG ATLCGYYIPP SAVVVTQNWS LHGSPKVWKD
     PHTFDHTRWL PGSSLSEEAK ISFNPFGQGA RQCLGIHLGW MQLRLATALF FRRCPGAKLA
     PSTTPESMVM IDSFIAGMPK ARRCAIQL
 
 
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