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easF

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Claviceps fusiformis
Length
355 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:17720822). However, cloA does not encode a functional enzyme indicating that C.fusiformis terminates its ergot alkaloid pathway at elymoclavine (PubMed:17720822).
Similarity
Belongs to the methyltransferase superfamily.
Mass
39.955 kDa
Sequence
MPACSVTDIRSHVVEDSLPDQVIKGLKSSPKTLPALLFYSNEGLDHWNHHVSQPDFYPRHQEVDILKQRGDEMARAIAPNSVILDLGSANLEKVVHLLKALEAQGKDVTYFALDISAPQLEVTLNEIPTSEFRHVRFAGLHGTFEDGLRWISETPHICDLPHCVLLLGLTIGNFSRASAATFLGNIASQALRGASKDQSSILMSLDSCKVPTQILRAYTSNGVEPFALQSLTFAKTLLRGPMLHNDSDEPLPCYLQPDDWYYHSEWNFVLGRHEASLIPRYRDVHLGSLLQDITVKKDEKIRFGCSYKYDDMERHQLFLDAGVEQDVAWTNEGCDVVIYELKKRSNTEKLGIDRN

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Claviceps purpurea (strain 20.1)
Length
344 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.54 kDa
Sequence
MPALPVIDIRSNHVEDSLPEQIIKGLTSQPKTLPPLLFYSNEGLEHWNHHSRQPDFYPRRQEIEILKQGGNDIARSIAPSSVILDLGSANLEKVGYLLEALEAQEKDVLYFALDISAPQLATTLKEIPSSNFRHVRFAGLHGTFEDGLRWINETPEIRDLPHCVLLLGLTIGNFSRQNAAAFLQNIANHALTGASKNKSSILLSLDSCKVPTKVTRAYTSDGVVPFALQALTYAKALLCDRIDNGIDEKVLSCNLRPEHWHYLSEWNFALGRHEASLIPRFGDVCLGSMLQDIIVKKEEKVRFACSYKYDAKERQKLFLDSGVDQGMVWTNEGCDVAIYELKLA

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Claviceps purpurea
Length
344 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.512 kDa
Sequence
MPALPVIDIRSNHVEDSLPEQIIKGLTSQPKTLPPLLFYSNEGLEHWNHHSRQPDFYPRRQEIEILKQGGNDIARSIAPSSVILDLGSANLEKVGYLLEALEAQEKDVLYFALDISAPQLATTLKEIPSSNFRHVRFAGLHGTFEDGLRWINETPEIRDLPHCVLLLGLTIGNFSRQNAAAFLQNIANHALTGASKNKSSILLSLDSCKVPTKVTRAYTSDGVVPFALQALTYAKALLCDRIDNGIDEKVLSCNLRPEHWHYLSEWNFALGRHEASLIPRFGDVCLGSMLQDIVVKKDEKVRFACSYKYDAKERQKLFLDSGVDQGMVWTNEGCDVAIYELKLA

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Epichloe festucae var. lolii
Length
344 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). The presence of easA is not required to complete this reaction (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.608 kDa
Sequence
MSKPNVLDIRLATFEDSIVDLVINGLRKQPKTLPALLFYANEGLKHWNHHSHQPEFYPRHQEVQILKKKAQEMAASIPMNSVVVDLGSASLDKVIHLLEALEVQKKNISYYALDVSASQLESTLAAIPTQNFRHVRFAGLHGTFDDGLHWLKEAPEARDVPHTVLLFGLTIGNFSRPNAAAFLSNIGQHAFQGKSGDQCSILMSLDSCKVPTQVLRAYTCEGVVPFALQSLTYANGLFSEKNKTQASGDVQHKVFNLDEWYYLSEWNFVLGRHEASLIPRSKDIKLLPPLDGILVSKDEKVRFGCSYKYDQEERMELFAAAGVKNEVTWSDEGCDVAFYQLKLS

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
Length
340 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (PubMed:22403186). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.039 kDa
Sequence
MGSINPPQILDIRRSKFEESIPKQVEAGLLSSPKTLPALLFYSTEGIQHWNRHSHASDFYPRHEEIQILKDKATDMAASIADGSVVVDLGSASLDKVIHLLEALEAAQKKVTYYALDLSFSELTSTLQAIPTDQFVHVQFSALHGTFDDGLQWLKETPVIRDQPHCLLLFGLTIGNFSRSNAAKFLHNIASHALVESPSQSSILLTLDSCKVPTKVTRAYTAEGVVPFALESLKYGNTLFQQDGGENVFDPEDWYFLSEWNYVLGRHEASLVPRSKDIKLGRPLDKIVVGKHEKVRFGCSYKYDSEERKELFGTAGLRDVKSWSKEGCDVAFYQLKCCPN

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Arthroderma otae (strain ATCC MYA-4605 / CBS 113480)
Length
340 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (PubMed:22403186). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.134 kDa
Sequence
MGNTNPPHILDIRRSKFEESIPKQVEAGLLSSPKTLPALLFYSTEGIQHWNRHSHAPDFYPRHEEIQILKEQATDMAASIADGSVVVDLGSASLDKVIHLLEALEAAQKKVTYYALDLSFSELTSTLQAIPTEQFIHVQFSALHGTFEDGLHWLKETPVIQDQPHCLLLFGLTIGNFSRPNAAAFLRNIASQALTGSPSQSSILLTLDSCKVPTKVTRAYTAEGVVPFALESLRYANTLFPQDGEERVFDPHDWHFLSEWNYILGRHEASLIPQSRDIKLGSPLDRIVVAKHEKIRFGCSYKYDCGERKELFESAGLHDVKIWSKEGCDVAFYQLKCCPN

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Trichophyton verrucosum (strain HKI 0517)
Length
340 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (PubMed:22403186). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.117 kDa
Sequence
MGSINPPQILDIRRSKFEESIPKQVEAGLLSSPKTLPALLFYSTEGIQHWNRYSHASDFYPRHEEIQILKDKATDMAASIADGSVVVDLGSASLDKVIHLLEALEAAQKKVTYYALDLSFSELTSTLQAIPTDQFVHVQFSALHGTFDDGLQWLKETLVIRDQPHCLLLFGLTIGNFSRPNAAKFLHNIASHALVESPSQSSILLTLDSCKVPTKVIRAYTAEGVVPFALESLKYGNTLFQQDAGENVFDPEDWYFLSEWNYVLGRHEASLVPRSKDIKLGRPLDKIVVGKHEKVRFGCSYKYDSEERKELFGTAGLRDVKSWSKEGCDVAFYQLKCCPN

Gene
easF
Protein
4-dimethylallyltryptophan N-methyltransferase easF
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Length
339 amino acids
Function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Similarity
Belongs to the methyltransferase superfamily.
Mass
38.094 kDa
Sequence
MTISAPPIIDIRQAGLESSIPDQVVEGLTKEVKTLPALLFYSTKGIQHWNRHSHAADFYPRHEELCILKAEASKMAASIAQDSLVIDMGSASMDKVILLLEALEEQKKSITYYALDLSYSELASNFQAIPVDRFHYVRFAALHGTFDDGLHWLQNAPDIRNRPRCILLFGLTIGNFSRDNAASFLRNIAQSALSTSPTQSSIIVSLDSCKLPTKILRAYTADGVVPFALASLSYANSLFHPKGDRKIFNEEDWYFHSEWNHALGRHEASLITQSKDIQLGAPLETVIVRRDEKIRFGCSYKYDKAERDQLFHSAGLEDAAVWTAPDCDVAFYQLRLRLN