AFLK_ASPPU
ID AFLK_ASPPU Reviewed; 643 AA.
AC Q12062; A0A0F0I0N8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Versicolorin B synthase {ECO:0000303|PubMed:8662689};
DE EC=4.2.1.143 {ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203};
DE AltName: Full=5'-oxoaverantin cyclase {ECO:0000303|PubMed:14602595};
DE EC=4.2.1.142 {ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203};
DE AltName: Full=Aflatoxin biosynthesis protein K {ECO:0000303|PubMed:15006741};
DE Flags: Precursor;
GN Name=aflK {ECO:0000303|PubMed:15006741};
GN Synonyms=vbs {ECO:0000303|PubMed:8662689}; ORFNames=P875_00052980;
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 / MRNA], PROTEIN SEQUENCE OF 163-180 AND
RP 414-428, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=8662689; DOI=10.1074/jbc.271.23.13600;
RA Silva J.C., Minto R.E., Barry C.E., Holland K.A., Townsend C.A.;
RT "Isolation and characterization of the versicolorin B synthase gene from
RT Aspergillus parasiticus. Expansion of the aflatoxin b1 biosynthetic gene
RT cluster.";
RL J. Biol. Chem. 271:13600-13608(1996).
RN [2]
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 [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 PROTEIN SEQUENCE OF 41-66, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
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 [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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=1731640; DOI=10.1016/0003-9861(92)90366-5;
RA Lin B.K., Anderson J.A.;
RT "Purification and properties of versiconal cyclase from Aspergillus
RT parasiticus.";
RL Arch. Biochem. Biophys. 293:67-70(1992).
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=8784203; DOI=10.1021/bi960924s;
RA McGuire S.M., Silva J.C., Casillas E.G., Townsend C.A.;
RT "Purification and characterization of versicolorin B synthase from
RT Aspergillus parasiticus. Catalysis of the stereodifferentiating cyclization
RT in aflatoxin biosynthesis essential to DNA interaction.";
RL Biochemistry 35:11470-11486(1996).
RN [11]
RP GLYCOSYLATION.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=8995367; DOI=10.1074/jbc.272.2.804;
RA Silva J.C., Townsend C.A.;
RT "Heterologous expression, isolation, and characterization of versicolorin B
RT synthase from Aspergillus parasiticus. A key enzyme in the aflatoxin B1
RT biosynthetic pathway.";
RL J. Biol. Chem. 272:804-813(1997).
RN [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14602595; DOI=10.1128/aem.69.11.6418-6426.2003;
RA Sakuno E., Yabe K., Nakajima H.;
RT "Involvement of two cytosolic enzymes and a novel intermediate, 5'-
RT oxoaverantin, in the pathway from 5'-hydroxyaverantin to averufin in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 69:6418-6426(2003).
RN [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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: Versicolorin B synthase; 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:8662689, PubMed:15932995,
CC PubMed:1731640, PubMed:8368837, PubMed:8784203, PubMed:14602595,
CC PubMed:15006741). 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:14602595, ECO:0000269|PubMed:15006741,
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:1731640, ECO:0000269|PubMed:18403714,
CC ECO:0000269|PubMed:18486503, ECO:0000269|PubMed:8368836,
CC ECO:0000269|PubMed:8368837, ECO:0000269|PubMed:8434913,
CC ECO:0000269|PubMed:8662689, ECO:0000269|PubMed:8784203,
CC ECO:0000305|PubMed:15006741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S-3S)-versiconal hemiacetal = H2O + versicolorin B;
CC Xref=Rhea:RHEA:33859, ChEBI:CHEBI:15377, ChEBI:CHEBI:77950,
CC ChEBI:CHEBI:77951; EC=4.2.1.143;
CC Evidence={ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995,
CC ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-5'-oxoaverantin + H(+) = (1'S,5'S)-averufin + H2O;
CC Xref=Rhea:RHEA:35671, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:71537, ChEBI:CHEBI:77933; EC=4.2.1.142;
CC Evidence={ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995,
CC ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for 5'-oxoaverantin {ECO:0000269|PubMed:14602595,
CC ECO:0000269|PubMed:1731640};
CC KM=3.1 uM for versiconal (at pH 6.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:1731640};
CC Vmax=6.67 nmol/min/mg enzyme with 5'-oxoaverantin as substrate
CC {ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:1731640};
CC Vmax=0.15 umol/min/mg enzyme with versiconal (at pH 6.0 and 30
CC degrees Celsius) as substrate {ECO:0000269|PubMed:14602595,
CC ECO:0000269|PubMed:1731640};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:14602595,
CC ECO:0000269|PubMed:1731640};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:15094053, ECO:0000305|PubMed:15006741}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14602595,
CC ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:8662689,
CC ECO:0000269|PubMed:8784203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14602595,
CC ECO:0000305|PubMed:15932995}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8995367}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U51327; AAC49318.1; -; Genomic_DNA.
DR EMBL; U51328; AAC49319.1; -; mRNA.
DR EMBL; AY371490; AAS66012.1; -; Genomic_DNA.
DR EMBL; JZEE01000729; KJK60751.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12062; -.
DR SMR; Q12062; -.
DR STRING; 1403190.Q12062; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblFungi; KJK60751; KJK60751; P875_00052980.
DR KEGG; ag:AAC49318; -.
DR BioCyc; MetaCyc:MON-14040; -.
DR BRENDA; 4.2.1.142; 523.
DR BRENDA; 4.2.1.143; 523.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0046572; F:versicolorin B synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein;
KW Lyase; Reference proteome.
FT PROPEP 1..41
FT /evidence="ECO:0000269|PubMed:15932995"
FT /id="PRO_0000424163"
FT CHAIN 22..643
FT /note="Versicolorin B synthase"
FT /id="PRO_0000424164"
FT BINDING 84..85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 105..106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 171..174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 613
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 624..625
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 70271 MW; 4B903BA6A0F39D11 CRC64;
MGRNWFQVTA MAVVPVVGIM AAVNPTILSS AASSLPSLGA MFTSDDFASQ MDGRIQAQGL
LSSHFGMYGW PGQSFDYVIV GGGTAGLAMA RRLSQDGTAS VAVIEAGGFY ETDAGNATEV
PMYLFNYFFD NGKVKNPLFD WYQYTTPQPG LAQREMFYMQ GKTLGGSTAR GAMLYHRGSK
GAYDMWADHV GDDSYRWDKW LPYFQKSVHF SGPETNPRPA NATALNDNTA FTASGGPVHV
GYPFQVNAIS SWVDRALAKM GFPEAQGFSN GNLLGRSYIT HTINPYTRRR ETASSSYLRE
ALMESNNLNI FTRTLVKRVL FDDQNRATGV TVNTDGFEWQ IGARKEVILS AGVMRSPQLL
MVSGIGPKDH LEQLGIPVRS DLSGVGQNMQ DTIILGPTVP VKVESHSQLM GNKETLPRAI
REYNEQRKGL LTNPGQDYFA FEKHQPGMLK ESTAADIDAA FPDDWPTFSY IALDDTFVPQ
YDGKNYFSMS AALMTPFSRG TVTINSNDTA NPPIVDPQWL ADPRDQEMAV AAFRRCREIV
ASDVMREVVA GPEILPGPQY QTDEEILNYI AETSDAYYAG VGTCAMGKAD DPKAVVDSKA
RVLGVKGLRI VDASIFPFAI DGQPMGTVYA LAEKIAAEMM AGQ
