AFLJ_ASPPU
ID AFLJ_ASPPU Reviewed; 314 AA.
AC Q6UEG5; A0A0F0HZ42;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Versiconal hemiacetal acetate esterase {ECO:0000303|PubMed:15184162};
DE EC=3.1.1.94 {ECO:0000269|PubMed:15184162};
DE AltName: Full=Aflatoxin biosynthesis protein J {ECO:0000303|PubMed:15006741};
DE AltName: Full=Esterase A {ECO:0000303|PubMed:12749588};
GN Name=aflJ {ECO:0000303|PubMed:15006741};
GN Synonyms=estA {ECO:0000303|PubMed:12749588}; ORFNames=P875_00052989-2;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=12749588; DOI=10.1023/a:1023353025330;
RA Yu J., Chang P.K., Bhatnagar D., Cleveland T.E.;
RT "Cloning and functional expression of an esterase gene in Aspergillus
RT parasitcus.";
RL Mycopathologia 156:227-234(2002).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15184162; DOI=10.1128/aem.70.6.3593-3599.2004;
RA Chang P.K., Yabe K., Yu J.;
RT "The Aspergillus parasiticus estA-encoded esterase converts versiconal
RT hemiacetal acetate to versiconal and versiconol acetate to versiconol in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:3593-3599(2004).
RN [15]
RP PATHWAY.
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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: Versiconal hemiacetal acetate esterase; part of the gene
CC cluster that mediates the biosynthesis of aflatoxins, a group of
CC polyketide-derived furanocoumarins, and part of the most toxic and
CC carcinogenic compounds among the known mycotoxins (PubMed:15006741,
CC PubMed:15184162). The four major aflatoxins produced by A.parasiticus
CC are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and
CC aflatoxin G2 (AFG2) (PubMed:15006741). The first step of the pathway is
CC the conversion of acetate to norsolorinic acid (NOR) and requires the
CC fatty acid synthase subunits aflA and aflB, as well as the PKS aflC
CC (PubMed:15006741). AflC combines a hexanoyl starter unit and 7 malonyl-
CC CoA extender units to synthesize the precursor NOR (PubMed:18403714).
CC The hexanoyl starter unit is provided to the acyl-carrier protein (ACP)
CC domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699).
CC The second step is the conversion of NOR to averantin (AVN) and
CC requires the norsolorinic acid ketoreductase aflD, which catalyzes the
CC dehydration of norsolorinic acid to form (1'S)-averantin
CC (PubMed:10584035). The norsolorinic acid reductases aflE and aflF may
CC also play a role in the conversion of NOR to AVN (PubMed:15006741). The
CC cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of
CC AVN to 5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is
CC performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms
CC HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin
CC (AVF) by aflK that plays a dual role in the pathway, as a 5'-
CC oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as
CC well as a versicolorin B synthase in a later step in the pathway
CC (PubMed:15006741, PubMed:11055914, PubMed:15932995). The averufin
CC oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal
CC acetate (VHA) (PubMed:15006741). VHA is then the substrate for the
CC versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL)
CC (PubMed:15006741 PubMed:15184162). Versicolorin B synthase aflK then
CC converts VAL to versicolorin B (VERB) by closing the bisfuran ring of
CC aflatoxin which is required for DNA-binding, thus giving to aflatoxin
CC 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:15184162, ECO:0000269|PubMed:15528514,
CC ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
CC ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
CC ECO:0000269|PubMed:16461654, ECO:0000269|PubMed:18403714,
CC ECO:0000269|PubMed:18486503, ECO:0000269|PubMed:8368836,
CC ECO:0000269|PubMed:8368837, ECO:0000269|PubMed:8434913,
CC ECO:0000305|PubMed:15006741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-versiconal hemiacetal acetate + H2O = (2S-3S)-
CC versiconal hemiacetal + acetate + H(+); Xref=Rhea:RHEA:35715,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:77950, ChEBI:CHEBI:77975; EC=3.1.1.94;
CC Evidence={ECO:0000269|PubMed:15184162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-versiconol acetate + H2O = (S)-versiconol + acetate +
CC H(+); Xref=Rhea:RHEA:35719, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:72673, ChEBI:CHEBI:77947; EC=3.1.1.94;
CC Evidence={ECO:0000269|PubMed:15184162};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:15094053}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed.
CC {ECO:0000269|PubMed:12749588}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KJK60750.1; Type=Erroneous gene model prediction; Note=The predicted gene P875_00052989 has been split into 2 genes: P875_00052996-1 (aflH) and P875_00052996-2 (aflJ).; Evidence={ECO:0000305};
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DR EMBL; AY371490; AAS66011.1; -; Genomic_DNA.
DR EMBL; JZEE01000729; KJK60750.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q6UEG5; -.
DR SMR; Q6UEG5; -.
DR STRING; 1403190.Q6UEG5; -.
DR ESTHER; asppa-q6ueg5; Hormone-sensitive_lipase_like.
DR EnsemblFungi; KJK60750; KJK60750; P875_00052989.
DR KEGG; ag:AAS66011; -.
DR BioCyc; MetaCyc:MON-14036; -.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; TAS:UniProtKB.
DR GO; GO:0140397; F:versiconal hemiacetal acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..314
FT /note="Versiconal hemiacetal acetate esterase"
FT /id="PRO_0000424165"
FT MOTIF 85..87
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 154
FT /evidence="ECO:0000250|UniProtKB:P23872"
FT ACT_SITE 255
FT /evidence="ECO:0000250|UniProtKB:P23872"
FT ACT_SITE 285
FT /evidence="ECO:0000250|UniProtKB:P23872"
SQ SEQUENCE 314 AA; 34474 MW; E57D53180B398BDC CRC64;
METPFAGPWH QFVEDLGQTP CLPGKDLDSI LAGWGQLAGT LATRYGFPPP DESVATEDVQ
LDGLWLRCYT PANATGQEPV GLYFHGGGWV MGGVKEEDGF CRVISRQCQM RLVSVEYRKA
PETRYPGALN DGVSAALWAQ SRYENQPLVL MGTSAGGNLA FGTALRLIDQ DMADKVSGVV
ALAPITVHPD AVPEHLKEQY TAYEENAELT VNSRAAMQVF FDCYKAPVDD VYTSCLLHPR
LLALPKVYIA ELGLDTLRDD ARLMKGALDT AKVPVMYDAY PGYPHCSFMF PFKSLGEHQR
TFLGGVAKAV RWMS
