UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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A0A0F7TN69 | MLSRSHSNATMSTTRHRLLATASRFVETLESLDMDAMLAVRSSTCLHHMCCPSFRNYSITNDQTREALPQWKATIKKYKFGVLDDSQTLVDEQARKVMIRAETAAETTVGDYNNEYVFILRMTEDCNAVDEIWEFYDTIRLRDLRHRLEAGHVPIGVDAPAPFTTTASPAAL | Part of the gene cluster B that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the trt14 isomerase family. |
A0A0U5GHU6 | MTGTQILELFGPAPEPPSELGRYRILSPTAGIRVSPLQLGALSIGDAWSADLGSMDKDSAMALLDAYAASGGNFIDTANAYQNEQSETWIGEWMANRNNRDQMVIATKFGPDYRAHELGKGLAVNYSGNHKRSLHMSVRDSLRKLQTSWIDILYLHTWDYTTSVPELMDALHHLVQRGEVLYLGICNTPAWVVSAANTYAQQQGKTQFSVYQGRWNPLRRELERDILPMARHFGMAITVYDALGSGKFQSRKMLARRKDQGEGLRAIYGRQQTAQEEAMSNALGVVAAQHGIESVTAVALAYLLAKAPYVFPIIGGRKIQHLHDNIQALSLRLTHEEIKYLESVGDFDLGFPYDMVGVDPADTGMATPIVAQAAPMAFVQRSKAIGYSESNKGLSE | Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily. |
C8VQ93 | MTGTRILELFGPAPEPPSELGRYRILSPTAGIRVSPLQLGALSIGDAWSTDLGSMDKDSAMELLDAYAAAGGNFIDTANAYQNEQSEMWIGEWMASRGNRDKMVIATKFGTDYRAHELGKGLAVNYSGNHKRSLHMSVRDSLQKLRTSWIDILYLHTWDYTTSIPELMDSLHHLVQRGDVLYLGICNTPAWVVSAANTYAQQQGKTQFSVYQGRWNPLRRELERDILPMARHFGMAVTVYDALGSGKFQSRDMLARRKDQGEGLRAIYGGQQTALEEAMSKALGVVAAQHGIESVTAVALAYLLAKAPYVFPIIGGRKIQHLHDNIEALSLRLSQEEIEYLESVGDFDPGFPYDMAGVDPADTGIATPIVAQAAPMAFVQRSKAIGYAESSKGSQMFG | Aldo-keto reductase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. Impairs the synthesis of austinol and dehydroaustinol and accumulates the intermediate compounds preaustinoid A4, preaustinoid A5 and austinoneol A11 (PubMed:22329759). In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily. |
A0A0F7TN16 | MTGTRILELFGPAPEPPSELGRYRILSPTAGIRVSPLQLGALSIGDAWSTDLGSMDKDSAMELLDAYAASGGNFIDTANGYQNEQSETWIGEWMASRTNRDQMVIATKFGPDYRAHELGKGLPVNYSGNHKRSLHMSVRDSLRKLQTSWIDILYLHTWDYTTSIPELMDSLHHLVQRGEVLYLGICNTPAWVVSAANTYAQQQGKTQFSVYQGRWNPLRREIERDILPMARHFGMAVTVYDALGSGKFQSRDMLARRKDQGEGLRAIYGGEQTALEEAMSKALGVVAAQHGTESVTAVALAYLLAKAPYVFPIIGGRKIQHLHDNIQALSLRLSQEEIKYLESVGDFDPGFPYDMAGVDPADTGIATPIVAQAAPMAFVQRSKAIGYAESNKGSQTSG | Aldo-keto reductase; part of the gene cluster B that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily. |
A0A0U5GIU9 | MSHLTVSKILEDPFSALSLSEMLKILAALGWSTNYLAMAHRTHADRLPAIAVLPLCCDIAWEFTYAWIYPQASGHWQGVVRVWFFLHTAVLAATLRYAPNDWAGTPLGKSRARLVLLYVAVIGAFAAGQLCLALEMGGALGFHWGGALCQFLSSSGAVGQLLTRGHTRGASLVIWGARAISTAGGFVKLCIRFQHQVDGAPWLDSPMCWFYIGIVLSLDASYPVLYQLTRRHEEASGRGNSGKVKNR | Terpene cyclase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). Secondary metabolite biosynthesis; terpenoid biosynthesis. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the paxB family. |
C8VQ96 | MSQLTISKIIEEPFSALSLSEMLKILAALGWSTNYLAMVYRTQADKLPAIAVLPLCCDIAWEFTYAWIYPQASGHWQGVVRVWFFLHTAVLAATLRYAPNDWAGTPLGESRGRLVLLYAAVIAAFAAGQLCLALEMGGALGFHWGGALCQFLSSSAAVGQLLTRGHTRGASLLIWGARAISTAGGDRALIGCVVSGAVPIDQKA | Terpene cyclase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Impairs the synthesis of austinol and dehydroaustinol (PubMed:22329759). In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the paxB family. |
A0A0F7TZE0 | MEEPLTVAAIFRGPFNILAISEVLKVVAAVGWSVNYIGMVHRAWKDQIPSIGILPLCCDIGWEFVYAWMFPDFSSHWQGVVRVWFFLHSAVLLVTLKVSPNDWANTPLAHRHIVFIYIFVTIVFGAGQYALAAEIGPALGFHWGGALCQFLSSSGGIAQLLSRGHTRGASYLIWFARAISTFAGFIKLCIRFQHNVDGAPWLDSPMCWFYIVTVLSFDAAYPFLYFSMRKFETPAPQREARIKKQ | Terpene cyclase; part of the gene cluster A that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the paxB family. |
A0A0U5CJU6 | MSDTSATKTEIRVIIVGGSVAGLTLAHCLAKANISHVVLEKRAEISPQEGAFLGIWPNGGRIFDQLGVYADLEQCTVPIHTMRVRFPDGFSFSSELPRCVQERFGYPIVSLDRQKVLEILHDRYPAKSNIHINKRVTEIRQTEREAQVVTDDGAVYKGDLVVGADGIHSAVRAEMWRQAKGLVGRRDGQAFAVEYACVFGISTPIPGLESGEHVNSYSDGLCVITFHGKDGRIFWFILIKLHKRFVYPKTPRFSASDAAKVCAEYASVPVWGEICVRDLWRNKTSASMTALEEGLLKTWNFKRVVLLGDSIHKMTPNIGQGANTAAEDAAVLASLLQRLSTSASSTTSGTIDAVLREYVSLRYKRVKSTYQRAYFGARLHTRDNVLKCFVGRYIFPRFSQQVLERTSQAIAGAPLVDFLPTPKRSGAGWSDYAGSPEVGAPTVPWLVISLPVLASVLCYLMFA | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). Secondary metabolite biosynthesis; terpenoid biosynthesis. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the paxM FAD-dependent monooxygenase family. |
C8VQ98 | MSDTPTRKTDLRVIIVGGSVAGLTLAHCLANANIDHIVLEKRAEISPQEGAFLGIWPNGGRIFDQLGVYADLEKCTVPIHKMRVRFPDGVSFSSELPRQVQERFGYPIISLDRQKVLEILYNRYPAKSNIHVNKKVTEIRQTEREAQVLTADGAVYKGDLVVGADGIHSAVRAEMWRQAKDLVGRRDRQDVNHEIAAFTVEYACVFGISSPISGLESGEHVNSYSNGLCVITFHGKDGRVFWFILIKLQKRFIYPFTPRFSASDAAKICAEYANVPVWGDICVRDLWGNKTSVSMTALEEGLLETWRFKRVVLLGDSIHKMTPNIGQGANTAAEDAGVLASLLQRLSTSDSSATSCTIDAVLQEYASLRYERVKSTYQRAYFGARLHTRDDALKAFVGRYIFPRFRQQVLERTSQAIAGAPQVDFLPTPKRTGPGWSDYAGSPEVGAPTLPWLVISLPVLASMLCYLVYSSVFVTPIFP | FAD-dependent monooxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Impairs the synthesis of austinol and dehydroaustinol (PubMed:22329759). In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the paxM FAD-dependent monooxygenase family. |
A0A0F7TXA0 | MSQATVEEKSKLRVIIVGGSVAGLTLAHCLAKANIDHIVLEKRAEISPQEGAFIGIWPNGARIFDQLGLYEDFESLTPPVHRMNVRFPDGFTFSSYLPRTIQERFGYPIISIDRQKVLETLYERYPHKSNVLVNKKVMNVRFSGKGVSVVTEDGSAYDGDLVVGADGIHSRIRSEMWRLADENHPGLITSQDKQAFTVEYACVFGISEQLPSLPAGEHINSYSNGLCVITFHGEKGRIFWFLLVKLPEKTTYPNTPRFSASDAASLCNKFARFRVSEDICVSDLWMHKLFASMTALEEGILERWHYDRIVLLGDSVHKMTPNIGQGANTALEDASVLASLLNNLSKLSTEDGTSAYAMTKLLNEYQSTRYERAKNTHDKSRFGARLHTRDDMIKTLIGRYVFPYAGPRVLERSVKSLATAHSVEYLPFPKRLGPAWGEYSSPNKSTLGSTPIHMLTLLLPCLFYFMYSKLNLFVSL | FAD-dependent monooxygenase; part of the gene cluster A that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the paxM FAD-dependent monooxygenase family. |
A0A0U5CJV1 | MCMQEYSTCPTIDHDGLHKICCYSHSQHDCRDPVIDMPPCCYPTLVRKQKMTVNPGSKSHHPKAGLLSYLPAALVPYGELLRVHRALGYYLNTSPYVVGIAYSAATAPTKLPLDLLLDRLLLLTLWSFILRSAGCAWNDLIDVDIDRQISRTQSRPLARGAISLPTATIFTACLFALGCSLFLFLPRQCAFEAGIEVFFALLYPFGKRFTDHPQLILVNIAWAIPMAMHSLGVEPGRQILSSICLCVFIATVIVLIDLVYSRQDTEEDLKVGVKSMAVRYRDCIDTLAYSLFAISTLALLFGGLLGGLRAPFVVFSVGGHIVGFWTFLRASLQTGPAGVESRAKSSCLMASIFWLLGLGIEYAVRV | Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). (2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-carboxylate + diphosphate + H(+) Secondary metabolite biosynthesis; terpenoid biosynthesis. Impairs the biosynthesis of calidodehydroaustin and accumulates the intermediate compound 3,5-dimethylorsellinic acid. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the UbiA prenyltransferase family. |
C8VQ99 | MAVISELKRHHPKTGLLRYLPTGVVPYGELVRIHRALGYYLNTSPYVVGIAYTAATAETKLPLDLLLDRLLLLTLWSLILRSAGCAWNDLVDVDIDRQISRTQSRPLPRGAISLSAATIFTACLFVLGCSLLLFLPRECLFDAGIKVFFALLYPFGKRFTDHPQLILINIAWAIPMAMHSLGMEPSSQILSMLCMCVFFSAVIVMIDLVYSRQDTEEDLKVGVKSMAVRYRNCVETMAYSLFAISSLALLFGGVLGGLRVPFVLFSVGGHIVGFWRFLRASLQAGPAGVESRAKSSCLIASVFWVLGLGIEYAEMVKEKDNPTDKKKHPH | Polyprenyl transferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). (2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-carboxylate + diphosphate + H(+) Secondary metabolite biosynthesis; terpenoid biosynthesis. Impairs the synthesis of austinol and dehydroaustinol and accumulates the intermediate compound 3,5-dimethylorsellinic acid (PubMed:22329759). In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the UbiA prenyltransferase family. |
A0A0F7TXA1 | MPTKGDYQPPKNGILSKLPESTVPYGELLRIHRPLGYYLNISPYVVGVAYTAAISPVTLPATFLLGRLVILSLWGFCIRSAGCAWNDLIDMDIDRQVSRTKLRPLPRGAVSPSGAALLTAFMFGCGGSLLLLLPSQCAFEAAIVVFFALLYPFGKRFSDHPQLILTNIAWAIPMAMSSLDMNPLDFPIPTLAMSFSIASVIVMIDIVYACQDAEEDKKVGARSMAVRYMEITDQIAYSLFFSGTLSLLAGGILRGLGIPFLIFSVGGHFVGFLRFLRASLGNGAKSALVESRAKSSCLLATVFLVFGLFFEYCVRL | Polyprenyl transferase; part of the gene cluster A that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). (2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-carboxylate + diphosphate + H(+) Secondary metabolite biosynthesis; terpenoid biosynthesis. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the UbiA prenyltransferase family. |
A0A0U5GFR4 | MKIPDNPQIQRFPATTPAPTLWKAVADDGVAIVTNAIPIDTIQRFHADIDNTGHATYLEDYKAFKDKEFPVQAKHASNLVRTSPVFRHEILNTPLIHEICTAAFQHLGDYWLTSSIFRSTNPGNPAQDFHRDALFHPLLQYQSPSAPHLTVSLIIPTTPFTKANGATRVILGSHKWENMTPQNIDALSKDDSVHAEMNAGDIMILHQRTIHAGGEHLPEAKDTRRLLLLLFTSCQLAQLESALALPRPLVESLTPLAQKMVGWRTVKPAGVNVVGLNTYHTGTLEDGLGLRSNQTMAG | Iron/alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the PhyH family. |
A0A0U5GIM7 | MEVVRYFTSNQKQPPATGPKDSIVQLPDIPPVYECNVEVALRFDSVLDPEKLQQSLKRLLEIGNWRQLGGRLRRRDTNSDACGYDLHVPVEFTTERPAFIYKTLESPAAVDEHPVACKMPQPTDPNKILFYNVRDALTPSMTRTHHPRKAQEWAESDLPPLSFEQLNFRDGTIILLLFPHILMDATGYGLFLKAWTCVLQGRMDDVPQCCGFSESITDMLCHKTPAESFTWHNHLLKGLDRLRFTARLLWENICGKEERIIRVPGKFITQTRDKTLADLSTSQDSPFVSHSDVLVAWFVRVVLASLNPQHQRTLVLTNAFDIRHMLPPERAYLQNSVFLAHTMLPVGEVVSNPASFLANEIRRSLVRERTEEQVQARCAWAKDVGIMPLLGSSDMLLCNVSNWSKGGLLDLDFGPAAITQRPGPCVPSSILNCSQMRGVTPEYGIILGKDSQDGWWMQWRLSKFCWAMIERELDTINQTR | O-acyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. Leads to complete loss of production of austin. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the plant acyltransferase family. |
A0A0F7TQP2 | MEVVRYFTRNQKQLPATGPNDSIVQLPDIPPCYECNVEVALRFDSSLDSEKLQQSLKQLLEIGNWRQLGGRVRRRDTNPSACNYDLHVPAEFTTERPAFNYQIWELSGAIDEHPTASKMPRPTDPKKVSFYNVGDARSPLRTRTRYPRKAQEWADSDLPPLSFEQLSFRDGTIILLVFPHILMDATGYGLFLKAWTSVLQGRIDHVPQCCGFSESTTDMLGHKTPAGAFTWHNHLLKGLDSLKFTAGLLWENRWGKEDRVIRVPAKFIMHTRDKVLADLSTSQPSPFVSQSDVLIAWFTRVVLAALKPLQRRTLVLTNAFDTRHMLPPERAYLQNSVCMAHTMLPVGEVLYNPVSFLANEIRRSLVRERTEEQIQARCAWAKDVGIMPLLGTSDMLLCNVSNWSKGNLVDLDLCHAAVTEHRGPCVPSSILNCSQMGGVTPNYGIILGKDSQDCWWMQWHLPKFCWAGIERELDTINQIRWE | O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the plant acyltransferase family. |
A0A0U5GJY1 | MPSSSDFEAFTLTPLDQANGQVFFFYSLSYRVQDEASALHTIHKAIDLLLEKAPFLNGEIVFATDGLEVRPPTTDSEDRVPLVQVKRHSNRTLPVEKLGQSPFNVPRNFPLDALFNPLAALPTPDRPTPVIRFQVNLVNDGLVLTIGFNHAVFDALGAAVIVKLLAESCRNPANVGREGSLEIASTQSRVRSPLLALTSRWKKLDRVRADAPSSPEVTAVPPPLTDECFVFCADKLQRLRAACNSILCQLNENQKLLAGQPDVRFLSTNDVLTALICETIAQARHAARHTCRDEGLHPESTVSECLMAVNIRKFVDPPLPDDYMGNAGIPLRFQIETRRDAEPDLPRAFQEANPGLNTSSFLAIAETAYTIRIKLASFGDSYIDSLRSFLNADESQTAVHVLPACAIVSSLRHIKTYELQFGAELGEIRTFETGIPWVNGSCVILPLCANSSEVAGSAPWNVRITLDEGTMYCFKNEPALRWALWEQGRSKVPGSCDCKADA | O-acyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the fumigaclavine B O-acetyltransferase family. |
Q5AR30 | MPPSPDFEAFSLTPIDQANGQVFFFYNISYRVRNEASALQTIHNAIDVLLEKVPFLNGEIAFPAPVPDANNVLIVRPPRAKSEDQVPLVQVKRHSNCALPVKKLEQSPFNVPSSLPLNGLFNPLAAYPTPNRPTPVIRFQINLVNDGLILTLAFNHAVFDALGAAVIVKLLAESCRNQDKIGMDGRLGIPSTQARVRSPLLALSSRLKKNNRARVDAPSPSEFSENISHRPVAAPPPLKDECFVFCAEKLQQLRIACTSILEKLHENQKSVTGQGDVRFLSINDVLTALICESIAQARHAAKHPYRDEKLHAKPSVSECLMAVDLRKFVEPPLPHDYMGNAAIPLRFEVSSQRHASPDFHRAVREVPTGLNTSFFLAIAKTAYTIRAKLARFGESYIDSLSSFLNAHEEQKAVNILPACAIVSSLRHIKTYELQFGAELGEIQAFETGIPWVNGSCIILPLCANSSDVAGSAPWNVRITLDESTMYCFKNEPALRWALLEQGKSKVLGPCDCKADV | O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the fumigaclavine B O-acetyltransferase family. |
A0A0F7TSZ1 | MPSSSDFEAFALTPLDQANGQVFFFYSISYQVQNEASALRTIHNGIDVLLERVPFLNGEIAFAAAVPGANNILTVRPPTANSKDQVPLVKVKRHSNRTLPVEKLEQSPFNVPRNLPLDGLFNPLAAFPTPDRPTPVIRFQINLVNDGLILTLAFNHAVFDALGAAVIVKLLAESCRNQENIGMAGSMGIPSTQARVQSPLLALSSRLKKHNHVHANAPSSSEVSETISQRPVTAPPPLTDECFVFCAEKLQQLRIACASILGKLNENQKSRAGQGDIRFLSSNDVLTALICESIAQARHAAKHTCRDEDLHAKSSVSECLMAVNLRKFVEPPLPDDYMGNAGIPLRFEVRTQRQAAPDFHPAIREVPPGLNTSSFLAIAKTAYTIRAKLARFGESYIDSLSSFLNADESQTAVNVLPACAIVSSLRHIKTYELQFGVELGEIQTFETGTPWVNGSCMILPLCANSSDVAGSAPWNVRITLDEGTMDCFKNEPALRWALWDQAKSKVPGSCNCMTDA | O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives. Belongs to the fumigaclavine B O-acetyltransferase family. |
Q56830 | MDPIRSRTPSPARELLPGPQPDRVQPTADRGGAPPAGGPLDGLPARRTMSRTRLPSPPAPSPAFSAGSFSDLLRQFDPSLLDTSLLDSMPAVGTPHTAAAPAECDEVQSGLRAADDPPPTVRVAVTARPPRAKPAPRRRAAQPSDASPAAQVDLRTLGYSQQQQEKIKPKVRSTVAQHHEALVGHGFTHAHIVALSQHPAALGTVAVTYQDIIRALPEATHEDIVGVGKQWSGARALEALLTEAGELRGPPLQLDTGQLLKIAKRGGVTAVEAVHAWRNALTGAPLNLTPDQVVAIASNIGGNQALETVQRLLPVLCQAHGLTPDQVVAIASHGGGKQALETVQRLLPVLCQAHGLTPDQVVAIASNIGGKQALATVQRLLPVLCQDHGLTPDQVVAIASHGGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNIGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNIGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNNGGKQALETVQRLLPVLCQTHGLTPDQVVAIANHDGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNIGGKQALATVQRLLPVLCQAHGLTPDQVVAIASHDGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNNGGKQALETVQRLLPVLCQDHGLTPAQVVAIANHGGGKQALETVQRLLPVLCQDHGLTPVQVVAIASNSGGKQALETVQRLLPVLCQDHGLTPVQVVAIASNGGGKQALATVQRLLPVLCQDHGLTPVQVVAIASHDGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNGGKQALESIVAQLSRPDPALAALTNDHLVALACLGGRPALDAVKKGLPHAPELIRRINRRIPERTSHRVADLAHVVRVLGFFQSHSHPAQAFDDAMTQFGMSRHGLAQLFRRVGVTELEARYGTLPPASQRWDRILQASGMKRVKPSPTSAQTPDQASLHAFADSLERDLDAPSPMHEGDQTRASSRKRSRSDRAVTGPSTQQSFEVRVPEQQDALHLPLSWRVKRPRTRIGGGLPDPGTPIAADLAASSTVMWEQDAAPFAGAADDFPAFNEEELAWLMELLPQSGSVGGTI | Avirulence protein. Induces the hypersensitive response (HR)in rice plants carrying the resistance gene Xa10. Activity depends on the presence of the core repeat domains; replacement with repeat domains from other proteins (AvrBs3 of X.euvesicatoria (AC P14727) or AvrXa7 of this organism) does not elicit the HR. Probably acts as a transcription factor in its host plant (rice) to induce plant resistance or disease. Secreted via a type III secretions system (TTSS). Localizes to the plant cell nucleus. The central DNA-binding region is composed of 23.5 tandem core repeats with 1 base-specifying residue (BSR residue 13, also called repeat variable diresidue, RVD, residues 12 and 13) each of which recognizes 1 base in the target DNA. The BSR is probably the only residue which contacts DNA in a sequence-specific manner. The activation domain activates transcription of a reporter gene upon expression in planta and in yeast. The 3 putative nuclear localization signals seem to be highly redundant; only mutation of all 3 knocks out the HR. By combining the central DNA-binding domain with the catalytic domain of the restriction endonuclease FokI, TALE-nuclease (TALEN) enzymes able to target specific dsDNA sequences can be created that enable eukaryotic genome modification. Other potential uses as transcriptional repressors, for transposon targeting, DNA methylation or histone tail modifictions are also possible. Belongs to the transcription activator-like effector (TALE) family. |
Q76C74 | MFNRFNKLQAALALVLYSQSALGQYYTSSSIASNSSTAVSSTSSGSVSISSSIELTSSTSDVSSSLTELTSSFTEVSSSIAPSTSSSEVSSSITSSGSSVSGSSSITSSGSSVSSSSPYDERFNSLDLSVHVSAGFSAGVSVGLEPSATTASVTTTLSPYDERVNLIELGVYVSDMRAHLVEYLLFQAAHSTEPHPTEIAAAFLDHGDFTTRLTGISGDEVTRMITGVPWYSTRLKPAISEALAKDGIYTAIPTSTSTTSDTYISSSSPSQVTSSAEPTTVSGVTSSVEPTRSSQVTSSAEPTTVSEITSSAEPLSSSKATTSAESISSNQITISSELIVSSVITSSSEIPSSIEVLTSSGISSSVEPTSLVGPSSDESISSTESLSATSTPLAVSSTVVTSSTDSVSPNIPFSEISSSPESSTAITSGSSSATESGSSVSGSTSATESGSSASGSSSATESGSSVSGSTSATESGSASSVPSSSGSVTESGSSSSASESSITQSGTASGSSVSSTSGSVTQSGSSVSGSSASSAPGISSSIPQSTSSASTASGSITSGTLTSITSGSSSATESGSSVSGSSSATESGSSVSGSTSATESGSSVSGSTSATESGSSASGSSSATESGSSVSGSTSATESGSSVSGSTSATESGSSASGSSSATESGSASSVPSSSGSVTESGSSSSASESSITQSGTASGSSASSTSGSVTQSGSSVSGSSASSAPGISSSIPQSTSSASTASGSITSGTLTSITSGSSSATESGSSASGSSSATESGSSVSGSTSATESGSSVSGSTSATESGSSASGSSSATESGSSVSGSTSATESGSSASGSSSATESGSASSVPSSSGSVTESGSSSSASESSITQSGTASGSSASSTSGSVTQSGSSVSGSSASSTSGSVTQSGSSVSGSSASSAPGISSSIPQSTSSASTASGSITSGTLTSITSSASSASATASNSLSSSDGTIYLPTTTISGDLTLTGKVIATEGVVVAAGAKLTLLDGDKYSFSADLKVYGDLLVKKSKETYPGTEFDISGENFDVTGNFNAEESAATSASIYSFTPSSFDNSGDISLSLSKSKKGEVTFSPYSNSGAFSFSNAILNGGSVSGLQRRDDTEGSVNNGEINLDNGSTYVIVEPVSGKGTVNIISGNLYLHYPDTFTGQTVVFKGEGVLAVDPTESNTTPIPVVGYTGENQIAITADVTALSYDSATGVLTATQGNSQFSFSIGTGFSSSGFNVSEGTFAGAYAYYLNYGGVVASSATPSSTSTTSGATNSTSGSTSFGASVTGSTASTSFGASVTGSTASTLISGSPSVYTTTLTYATTTSTVVVSCSETTDSNGNVYTITTTVPCSSTTATITSCDETGCHVTTSTGTVATETVSSKSYTTVTVTHCDNNGCNTKTVTSEAPEATTTTVSPKTYTTATVTQCDDNGCSTKTVTSECPEETSATTTSPKSYTTVTVTHCDDNGCNTKTVTSEAPEATTTTVSPKTYTTATVTQCDDNGCSTKTVTSECPEETSATTTSPKSYTTVTVTHCDDNGCNTKTVTSEAPEATTTTVSPKTYTTATVTQCDDNGCSTKTVTSEAPKETSETSETSAAPKTYTTATVTQCDDNGCNVKIITSQIPEATSTVTATSASPKSYTTVTSEGSKATSLTTAISKASSAISTYSKSAAPIKTSTGIIVQSEGIAAGLNANTLNALVGIFVLAFFN | Involved in cell wall organization and biosynthesis. Confers cell surface hydrophobicity (CSH). Covalently-linked GPI-modified cell wall protein (GPI-CWP). The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. Half of the downstream region (residues 1035 to 1713) of the AWA1 gene was lost in the nonfoaming strain K701 due to a chromosomal recombination event. Responsible for the thick foam layer formation on the sake mash during the fermentation process. 'Awa' means 'foam' in Japanese. Belongs to the SRP1/TIP1 family. Of froth and haze - Issue 78 of January 2007 |
Q6IEE4 | MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPERGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEATGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVGGVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKFQSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHALYMDALHKLFDQHKTHYGCSETQKLFFL | Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters (PubMed:15671038). Shows a strong preference for decyl alcohol (C10), with less activity towards C16 and C18 alcohols (PubMed:15671038). Shows a strong preference for saturated acyl-CoAs (PubMed:15671038). a fatty acyl-CoA + a long chain fatty alcohol = a wax ester + CoA (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl (9Z)-octadecenoate (9Z)-octadecenoyl-CoA + decan-1-ol = 1-O-decyl-(9Z)-octadecenoate + CoA (9Z)-hexadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-hexadecenyl (9Z)-octadecenoate + CoA (9Z)-octadecenoyl-CoA + octadecan-1-ol = 1-O-octadecyl (9Z)-octadecenoate + CoA (9Z)-octadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-octadecenyl (9Z)-octadecenoate + CoA hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate (9Z)-hexadecenoyl-CoA + hexadecan-1-ol = 1-O-hexadecyl (9Z)-hexadecenoate + CoA hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl octadecanoate (9Z)-octadecenoyl-CoA + eicosan-1-ol = 1-O-eicosanyl (9Z)-octadecenoate + CoA Predominantly expressed in skin, where it is limited to the sebaceous gland. Expressed in more mature, centrally located cells just before their rupture and sebum release. Also expressed in all tissues except spleen. Expressed at higher level in thymus, prostate and testis. Belongs to the diacylglycerol acyltransferase family. |
B2RW94 | MSCSMKTEHLQSLSLLQWPLSYVAMFWIVQPLLICLLFTPLWPLPTVYFVWLLLDWKTPDKGGRRSDWVRNWNVWNHIRDYFPITILKTKDLSPSENYIMGVHPHGLLTFGAFCNFCTEATGFSKTFPGITPHLATLSWFFKIPIIRDYIMAKGLCSVSQASIDYLLSHGTGNLVGIVVGGVGEALQSVPNTTTLLLKKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHEDSRMFKFQSLFRRIFGFYCCVFYGQGFHQDCKGLLPYHKPIITVVGEALPLPQVKNPSPEIVDKYHALYMDALYKLFEQHKVQYGCSNTQKLIFL | Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters (By similarity). Shows a strong preference for decyl alcohol (C10), with less activity towards C16 and C18 alcohols (By similarity). Shows a strong preference for saturated acyl-CoAs (By similarity). a fatty acyl-CoA + a long chain fatty alcohol = a wax ester + CoA (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl (9Z)-octadecenoate (9Z)-octadecenoyl-CoA + decan-1-ol = 1-O-decyl-(9Z)-octadecenoate + CoA (9Z)-hexadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-hexadecenyl (9Z)-octadecenoate + CoA (9Z)-octadecenoyl-CoA + octadecan-1-ol = 1-O-octadecyl (9Z)-octadecenoate + CoA (9Z)-octadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-octadecenyl (9Z)-octadecenoate + CoA hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate (9Z)-hexadecenoyl-CoA + hexadecan-1-ol = 1-O-hexadecyl (9Z)-hexadecenoate + CoA hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl octadecanoate (9Z)-octadecenoyl-CoA + eicosan-1-ol = 1-O-eicosanyl (9Z)-octadecenoate + CoA Belongs to the diacylglycerol acyltransferase family. |
Q6P437 | MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDWKTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHFATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMVIVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGGFVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIVAKYHTLYIDALRKLFDQHKTKFGISETQELEII | Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters (PubMed:15220349, PubMed:15671038, PubMed:16106050, PubMed:28420705). Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donors and acceptors, respectively (PubMed:15220349, PubMed:15671038). Also possesses acyl-CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-specific retinyl ester synthesis (PubMed:16106050, PubMed:24799687). Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13-cis-retinol, and all-trans-retinol substrates (PubMed:24799687). a fatty acyl-CoA + a long chain fatty alcohol = a wax ester + CoA all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA 1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoA all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl (9Z)-octadecenoate (9Z)-hexadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-hexadecenyl (9Z)-octadecenoate + CoA (9Z)-octadecenoyl-CoA + octadecan-1-ol = 1-O-octadecyl (9Z)-octadecenoate + CoA (9Z)-octadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-octadecenyl (9Z)-octadecenoate + CoA (9Z)-hexadecenoyl-CoA + hexadecan-1-ol = 1-O-hexadecyl (9Z)-hexadecenoate + CoA hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl octadecanoate 11-cis-retinol + hexadecanoyl-CoA = 11-cis-retinyl hexadecanoate + CoA (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA 11-cis-retinol + tetradecanoyl-CoA = 11-cis-retinyl tetradecanoate + CoA 9-cis-retinol + tetradecanoyl-CoA = 9-cis-retinyl tetradecanoate + CoA 13-cis-retinol + tetradecanoyl-CoA = 13-cis-retinyl tetradecanoate + CoA all-trans-retinol + tetradecanoyl-CoA = all-trans-retinyl tetradecanoate + CoA tetradecan-1-ol + tetradecanoyl-CoA = CoA + tetradecanyl tetradecanoate 11-cis retinoids act as allosteric modulators of acyl-CoA retinol O-fatty-acyltransferase (ARAT) activity by suppressing esterification of 9-cis, 13-cis, or all-trans retinols concurrently increasing the enzyme specificity toward 11-cis isomer. Monomer. Highly expressed in skin, where it is primarily restricted to undifferentiated peripheral sebocytes. Also expressed at lower level in other tissues except pancreas. Belongs to the diacylglycerol acyltransferase family. |
Q8BM49 | MFWPTKKDLKTAMEVFALFQWALSALVIVTTVIIVNLYLVVFTSYWPVTVLMLTWLAFDWKTPERGGRRFTCVRKWRLWKHYSDYFPLKMVKTKDISPDRNYILVCHPHGLMAHSCFGHFATDTTGFSKTFPGITPYMLTLGAFFWVPFLRDYVMSTGSCSVSRSSMDFLLTQKGTGNMLVVVVGGLAECRYSTPGSTTLFLKKRQGFVRTALKHGVSLIPAYAFGETDLYDQHIFTPGGFVNRFQKWFQKMVHIYPCAFYGRGLTKNSWGLLPYSQPVTTVVGEPLPLPKIENPSEEIVAKYHTLYIDALRKLFDQHKTKFGISETQELVIV | Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters (PubMed:15220349). Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donor and acceptor, respectively (PubMed:15220349). Also possesses acyl-CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-specific retinyl ester synthesis (PubMed:28096191). Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13- cis-retinol and all-trans-retinol substrates (By similarity). a fatty acyl-CoA + a long chain fatty alcohol = a wax ester + CoA all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA 1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoA all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl (9Z)-octadecenoate (9Z)-hexadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-hexadecenyl (9Z)-octadecenoate + CoA (9Z)-octadecenoyl-CoA + octadecan-1-ol = 1-O-octadecyl (9Z)-octadecenoate + CoA (9Z)-octadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-octadecenyl (9Z)-octadecenoate + CoA (9Z)-hexadecenoyl-CoA + hexadecan-1-ol = 1-O-hexadecyl (9Z)-hexadecenoate + CoA hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl octadecanoate 11-cis-retinol + hexadecanoyl-CoA = 11-cis-retinyl hexadecanoate + CoA (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA 11-cis-retinol + tetradecanoyl-CoA = 11-cis-retinyl tetradecanoate + CoA 9-cis-retinol + tetradecanoyl-CoA = 9-cis-retinyl tetradecanoate + CoA 13-cis-retinol + tetradecanoyl-CoA = 13-cis-retinyl tetradecanoate + CoA all-trans-retinol + tetradecanoyl-CoA = all-trans-retinyl tetradecanoate + CoA tetradecan-1-ol + tetradecanoyl-CoA = CoA + tetradecanyl tetradecanoate 11-cis retinoids act as allosteric modulators of acyl-CoA retinol O-fatty-acyltransferase (ARAT) activity by suppressing esterification of 9-cis, 13-cis, or all-trans retinols concurrently increasing the enzyme specificity toward 11-cis isomer. Monomer. Expressed in Mueller cells of the retina (at protein level) (PubMed:24799687). Abundant in tissues rich in sebaceous glands such as the preputial gland and eyelid (PubMed:15220349). Belongs to the diacylglycerol acyltransferase family. |
Q9VZM0 | MKTELRSCAACGEPISDRFFLEVGGCSWHAHCLRCCMCMCPLDRQQSCFIRERQVYCKADYSKNFGAKCSKCCRGISASDWVRRARELVFHLACFACDQCGRQLSTGEQFALMDDRVLCKAHYLETVEGGTTSSDEGCDGDGYHKSKTKRVRTTFTEEQLQVLQANFQIDSNPDGQDLERIASVTGLSKRVTQVWFQNSRARQKKHIHAGKNKIREPEGSSFARHINLQLTYSFQNNAQNPMHLNGSKAGLYPTHESSMDELSQDSSVHCMPSEV | Probable transcription factor. Required for the establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. First detected in neuroblasts in stage 9 embryos. Expressed in all 10 abdominal segments and in the labial segment during early embryogenesis. Expressed in the stage 14 developing epithelium. By embryonic stage 16, expression is refined to the abdominal histoblasts and salivary gland imaginal ring cells. Expressed in both larval and imaginal cells between the salivary gland and the salivary gland imaginal ring, in late third instar larvae. Also expressed in specific areas of the larval wing, leg and eye-antennal disks. Expressed in all stages of zygotic development, with highest levels of expression during embryonic and early pupal stages, and lower levels in larval and adult stages. |
P80948 | AWNRRSRSCGGVLRDPPGKIFNSDGPQKDCVWTIKVKPHFHVVIAIPPLNLSCGKEYVELLDGPPGSEIIGKICGGISLVFRSSSNIATIKYLRTSGQRASPFHIYYYADPEGPLPFPYFERQTIIATEKNIP | Mediates the binding of spermatozoa to component(s) of the egg's zona pellucida by a carbohydrate-binding mechanism. It is a secretory component of the male accessory glands being coated to the sperm surface at the time of ejaculation. Predominantly localized on the membrane overlying the acrosomal cap region of the sperm head. Belongs to the spermadhesin family. |
Q712L0 | MKLAAPSLALLLSTATLVSGAWNRRSRSCGGVLRDPPGKIFNSDGPQKDCVWTIKVKPHFHVVLAIPPLNLSCGKEYVELLDGPPGSEIIGKICGGISLVFRSSSNIATIKYLRTSGQRASPFHIYYYADPEGPLQFPYFDRQTIIATEKNIP | AWN proteins mediate the binding of boar spermatozoa to component(s) of the egg's zona pellucida by a carbohydrate-binding mechanism. Awn proteins are secretory components of the male accessory glands being coated to the sperm surface at the time of ejaculation. They possess as well heparin-, serine-protease-inhibitor-binding capability. Predominantly localized on the membrane overlying the acrosomal cap region of the sperm head. Partial N-acetylation differentiates isoforms AWN-1 (not acetylated) and AWN-2 (acetylated). Belongs to the spermadhesin family. |
Q6FPN0 | MSLITIFAFFIKATLVLSLDILTPTTLTGDQTFNEDVSVVSSLTLNDGSQYLFNNLLQIAPSSASVTANALAAVSVFTFSLPPSSSLSNSGTLIISNSNTGPSTEQHIVITPNVMANTGTITLSLAHTNTDSSSTLIIDPVTFYNTGTINYESIGSETNDPSLTGNILSIGSSGRTLQNLGTINLNAANSYYLLGTITENSGSINVQKGFLYVNALDFIGNTINLSTTTALAFISPVSQVVRVRGVFFGNIIASVGSSGTFSYNTQTGILTVTTNGVYSYDIGCGYNPALMSGQQETLSFQGNLYDTFLVLVNQPIPSDLTCAAVSSSITPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSSVEPSSPAVPSSSAEPSSSVVPPITPIPSSSVVSASVFDTSSTLPSSPTVPTSSVSPSSPTVPTSSVSPSSPTVPTSSESPSTLSTPSSSAAPSSFCPTCVSSGTPPAPSSSAVVPTSSAGGGNGGDNGQPGADGQPGAAGQPGAAGQPGAAGQPGAAGQPGAAGQPGAAGQPGAAGQPGAAGQPGAAGQPGAAGQPGAGSGGGSEQPTPGAGAGSGSADGNQSGTSSGTGNGQAGSGQAGSGQVGSGQAGAGQAGSGQAGAGQAGSGQAGAGQAGLDNTASGQSEGGQASAMDGDQSGRGGQSNSGSLLQPNAQQGTGSGTGSDTGADQASGESPGQIGDAQPGSGTDQSSGRHSLAAEARTSQSHSLAADARTRSTTRQTSVIAPGTAPGTAVVTTFHGCGTVNHKGMINILLALALLVLL | May play a role in cell adhesion. May be GPI-anchored. Induced during biofilm formation. |
Q6FNG1 | MRKLPLFMAWKFWLICLYIIKVASTQIVIKSNTIVGGNNPSGFQNGYIVSGDAFLAFQDMNTVPMYQTVRIDKGGALYYINNDKQGFSILSDHNYNHPFVFLNEGTVVVDDRRSISPGSWTIKDGSFTNNGNIMFTSSQGDIFSIGSNYITNTGFIFSKGTSFEKPQRLQIGNGNIWINTGTVCMANTTYILENAIQGGGCISVGENSVFNIYSFDMQQQTVYLSHPSSVLILNGGHEVPVYGLGNGNGILYPDAPIRDIYYDSSTGIMDVTAGTNGIYKFTVYIGAGYNESNFEIVSSIKIHGISYDNYNFVRYRGPPPNLAPSVCQPCVEIPLYSFQVPDPYTTTNELGFSETVSFYSTYNENDIPVIGNTTIYVPPAIYTLTKVNENTTETDIISRVTGMGYNGLPFTYYTTITVGEMETGVVTKTITITENKSRSTKTTLMSRNYTFSFSNYSPISSSGTYSVSTVDNITTLTDTVANVSSSGPNSIVTATMTTYQNNHEFNNASVINVTNSSNIMVPITSTFYSSVDSNLTTPITSLTRTSQSQIVSHITKLASSINETTIANTFPSPAASGTNYTTVVTNAEGSVQTDIVSHITTTDSDGKPTTIVSHITTTDSDGKPTTIVTTFPAPAASGADYTTVVTNADGSVETDIVSHITTKDSIGKPTTVVTTVPYTLCASNADYTTVVTKSNVSVETEVVSHITTTAPCSDLESHVENQTTSPSMHTTSLVGSENGVSAKTVNDKPNPTIFTEVAVSEGTTSNAGYVTDQGSSLEMFAPTGASAVESGNKVSQTQTASIFHGAGSTFKIKFNTILLSTSLTILILLGMA | Mediates cell-substrate adhesion and promotes biofilm formation. May be GPI-anchored. Induced during biofilm formation on catheters inside the host (PubMed:25406296). May be repressed during biofilm formation ex vivo (PubMed:21769633). |
B4UN32 | MISFVTLLAILGLLSISWADQTVRSVAGDQRVTDPVIVGDNSILDYYGGSNYDFSNNFEIGRGTLYIGKESYFSSFQSAPTDVPNSFHLLIKNTNNLQNNGQFIIENIKRHANQCSNSSIQVFPINFQNDGEFEIISGGVEGRCCLPTSVIAPQNFLNNGKFYYKVLTDTGSIYSGSCMQNVDIGASTTTTVNNNLWEFTGSINAQINGAVSGAAQINLDGSNMFVNANTFSGQVVNLINGGSFLQTSDPLSNIVVINGLGTSDTGVTSIAVKGKGKSFTYNPSSGIVKLTTVEGKTYAYQIGCGYNTKKFITNNDSGASYESADNFFVLTYSEPYSPQTCQLENSSIFSSNFISTSTSSSSSSSSASSLPSSMSSSLPSSLSSSLSSSLSSSMSSSMSSLFIIPPPYTTTRSSGSSIIDTEIVSFYSTTDSPGHTITGTTTTTLYGPHTHSSVSTPSSSSESSTTSNSSIESSSLPHTSVSSTPESSITPSSNTISSSPTSDFSSVQSSSIMESSSVVASSSVINSSSIVDSSSSSASSLPSSMSSSLSSSMSSSLPSSMSSSLSSSLSSSLSSSMSSSMSSLFIIPPPYTTTRSSGSSIIDTEIVSFYSTTDSPGHTITGTTTTTLYGPHTHSSVSTPSSSSESSTTSNSSIESSSLPHTSVSSTPESSITPSSNTISSSPTSDFSSVQSSSIMESSSVVASSSVINSSSIVDSSSSSASSLPSSMPSSLPSSMSSSLSSSMSSSLSSSLSSSLSSSMSSSMSSLFIIPPPYTTTRSSGSSIIDTEIVSFYSTTDSPGHTITGTTTTTLYGPHTHSSVSTPSSSSESSTTSNSSIESSSLPHTSVSSTPESSITPSSNTISSSPTSDFSSVQSSSIMESSSVVASSSATQSSSVINSSSIVDSSSSSASSLPSSMPSSLPSSLSSSLSSSLSSSMSSSMSSLFIIPPPYTTTRSSGSSIIDTEIVSFYSTTDSPGHTITGTTTTTLYESSIYSSSSSTIQESELSNTSRTTMTSNSSVSISSTSSRSSFSNTKSSTIVISQSASLPDSKTDIILSTSSNIGYSSRSLLSDLGTSISDSDIHHSVLHSTESYSSNESGTNPFTSIASLSNFIPESSSHTSTALGSENSVISSDILTTMSHPVATNSGDKPTTPKRSEQVSTTMTSSGPTPDTSSFDTDGMSAYSRPEFTTNSLEVNKSSTSQLGNNKQTFSNLQLESTRPHSENEVDNNTRLLQSIQQSSTYGTNNVNPLSPTGSISIPLTEDGQGDNNNWNSPATNDLCTQISFNLTATTITVTDRITITDSIHDISSEVITSYIYQTIVDQKTVTQTVDGKSLANKMSSIPKPSSRSLIQPQPPVAIELQEGAASTSRVSLVSLFISIILVLL | May play a role in cell adhesion. May be GPI-anchored. Truncated N-terminus. |
P33080 | MGFRLPGIRKTSIAANQASSKSVEVPKGYLVVYVGDKMRRFLIPVSYLNQPSFQDLLNQAEEEFGYDHPMGGLTIPCKEDEFLTVTSHLNDL | By auxin. Belongs to the ARG7 family. |
P33081 | MGFRLPGIRKASKAADAPKGYLAVYVGEKLKRFVIPVSYLNQPSFQDLLSQAEEEFGYDHPMGGLTIPCSEDVFQCITSCLN | By auxin. Belongs to the ARG7 family. |
P0C2K1 | ANKRPIWIMGHMVNAIYQIDEFVNLGANSIETDVS | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Contains 1 disulfide bond. Belongs to the arthropod phospholipase D family. Class I subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
P32293 | MAKEGLGLEITELRLGLPDAEHVAVANKNGEKKNKRVFSEIDDVGDENSSSGGGGDRKMENKNQVVGWPPVCSYRKKNSVNEASKMYVKVSMDGAPFLRKMDLGMHKGYSDLAFALEKLFGCYGMVEALKNVENGEHVPIYEDKDGDWMLVGDVPWEMFMESCKRLRIMKRADAKGFGLQPKGSLKGFIESVGK | Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). Homodimers and heterodimers. Found in elongating hypocotyls. By auxin and cycloheximide. The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV (By similarity). Belongs to the Aux/IAA family. |
P32294 | MESRVVFESDLNLKATELRLGLPGTEEKEDNNLRTHAVLRNNKRQVRETSQDSVSISKASHHQQHVETVSAPPPKAKIVGWPPIRSYRKNSVQEGEGDGIFVKVSMDGAPYLRKVDLKVYGGYPELLKALETMFKLAIGEYSEREGYKGSEYAPTYEDKDGDWMLVGDVPWDMFVTSCKRLRIMKGSEARGLGCVV | Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). Homodimers and heterodimers. Found in elongating hypocotyls. By auxin and cycloheximide. The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV (By similarity). Belongs to the Aux/IAA family. |
O24541 | MEKEDLGLEITELRLGLPGAGGENNTDKDKNKNKKRVFSDIEGENSSSEEDGKKETKNQVVGWPPVCSYRKKNTVNEPKLYVKVSMDGAPFLRKIDLAMHKGYSDLAFALDKFFGCYGICEALKDAENAEHVPIYEDKDGDWMLVGDVPWEMFRESCKRLRIMKRSDAKGFDLQPKGSLKGFIEGVRK | Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). Homodimers and heterodimers. By auxin. The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV (By similarity). Belongs to the Aux/IAA family. |
O24542 | MENSLGSYEKELNLKATELRLGLPGSDEPEKRATARSNKRSSPEASDEESISNGSDVTKEDNVVPPAKAQVVGWPPIRSYRKNNVQQKKEEESEGNGMYVKVSMAGAPYLRKIDLKVYKSYPELLKALENMFKCIFGEYSEREGYNGSEYAPTYEDKDGDWMLVGDVPWNMFVSSCKRLRIMKGSEAKGLGCF | Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). Homodimers and heterodimers. By auxin. The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV (By similarity). Belongs to the Aux/IAA family. |
O24543 | MGSYETELNLRATELRLGLPGSDEPQEKRPCSGSVVRSSNKRSSPELEESRCKSNINSDSSDSTTTSDHNEDSVQPAKVQVVGWPPIRSFRKNSLQQKKVEQGDGTGMYLKVSMAGAPYLRKIDLKVYKSYPELLKALQNLFKCTFGEYSEREGYNGSEYAPTYEDKDGDWMLVGDVPWNMFVSSCKRLRIIKGSEAKGLGCL | Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). Homodimers and heterodimers. By auxin. The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV (By similarity). Belongs to the Aux/IAA family. |
Q6HAM6 | MTKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFDLTEEEAKAVAVADKYLNQFLEADKVVFGFPLWNLTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKIALLNARGGVYSEGPAAEVEMAVKYVASMMGFFGATNMETVVIEGHNQFPDKAEEIITAGLEEAAKVANKF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q394J5 | MFKLLQIDSSPMGDASISRRLTQEYARNWLRAHPDGRVVERDLCRIAMPPIDAAWIAANFTPPDRRTAQQNEMLALSTTFTTELRDADEYVIGVPMHNWGPSAHFKLWLDHIVRQGETVETTPSGPRGLLGGRRATFVIAAGWRYGPDAERAQRNFLEPWLRTLFGFLGVEDMRFVMADGAADVFTGKADSAVFLAPHVDAVRALFA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q9HZ17 | MSRVLVIESSARQRGSVSRLLTAEFISHWKIAHPADRFQVRDLAREPLPHLDELLLGAWTTPCDGHSAAERRALERSNRLTEELRMADVLVLAAPMYNFAIPSSLKSWFDHVLRAGLTFRYAEQGPEGLLQGKRAFVLTARGGIYAGGGLDHQEPYLRQVLGFVGIHDVTFIHAEGMNMGPEFREKGLARARERMRQALETDTSLCVPLPTLR | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (PubMed:24915188). Shows a preference for naphthoquinones such as plumbagin (PubMed:24915188). Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:20417637). Preferred substrates are methyl red, amaranth and p-aminoazobenzene sulfonamide (PAABSA) (PubMed:20417637). 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Rate of quinone reduction is higher than reduction of azo substrates, suggesting the enzyme is better suited for carrying out quinone rather than azo reduction. Belongs to the azoreductase type 1 family. |
Q4KF31 | MTRLLHIQCSPRLRRSASLEIAHSFIQSYRQQRPDTEVTTLDLWSLDLPELDQTAMDAKYAQLAGQPLGNAEQRAWARLQALAEPLHQADLLVLSIPLWNFSIPYKLKHFIDLVSHQGILFSFDPENSLQGLLRNKTAVAAYARGLDFSSRSSTPAPAFDFQKPYIEAWLNFIGIANQHSLIVEKTILGPDIDQASRQAAAEQAQALAQQLAARQY | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q3KD08 | MKLLHIDSSILGDNSASRQLSSQVTKAWQAAEPSAVVTYRDLAADAISHFSSTTLVAAGTTAELRNAAQQHEAELSATTLAEFITADAIVVAAPMYNFTVPTQLKAWIDRIAVAGQTFRYTEAGPEGLCGGKKVVIVSTAGGIHAGQASGVAHEDYLKLVFGFLGITDIEVVRAEGLAYGEEVRNNAMSAAQAKISEQLFAAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q6KJM2 | MTKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFDLTEEEAKAVAVADKYLNQFLEADKVVFGFPLWNLTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKIALLNARGGVYSEGPAAEVEMAVKYVASMMGFFGATNMETVVIEGHNQFPDKAEEIITAGLEEAAKVANKF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q72X39 | MATVLFVKANNRPAEQAVSVKLYEAFLANYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFDLTEEEAKAVAVADKYLNQFLEADKVVFGFPLWNLTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKIALLNARGGVYSEGPAAEVEMAVKYVASMMGFFGATNMETVVIEGHNQFPDKAEEIIAAGLEEAAKVASKF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q630J1 | MTKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFDLTEEEAKAVAVADKYLNQFLEADKVVFGFPLWNLTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKIALLNARGGVYSEGPAAGAEMAVKYVATMMGFFGATNMETIVIEGHNQFPDKAEEIITAGLEEAAKVANKF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q390T2 | MARILVLKSSINGSQSQTSTLIDTFLAERQANGHADDVIVRNLVDADLPMLDSELFHALRGAANPSERAQRAIVLSDELIAELKGSDLLLIGAPMYNLNVPTQLKNWFDLVARARVTFRYTETYPVGLVEGISAIVFSSRGGVHVGQDTDAVTPYLRAVLGLMGIVDVEFVYAEGLDMKPHGFDAGLADARRQMDALHA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q4KEN7 | MNNLLLINASPRGQGSHGNQLALELVSSLRQRYPHLELVERDLGANPLPPLGMDYAHALTTPTPFDAPLFEVSEGLIGELERSDALLIATPMHNFTLPAALKLWIDYVLRIHRTFSSGPEGKVGLLKDRPVHVLVSSGGFHQGERARQPDFLTPYLRQVLNTLGLFDLQFTYLQGLVFGDEAVRATLDEARSALSLQPLFNPLVCA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q390D0 | MNNLLFVDASPHGSRSLGARIAREAIAQWQAAHPHARVVSRSLGQPGLPSISADYAHALVARQPDSDPALACSEQLIAEVEHSDGVLISTPMHNFTVPAALKLWIDFVLRIGRTFAATPEGKVGLLADRPVLVLVRSGGICRGAAARQPDFLTPYLKQVLAVIGFSTVDFIYLEGVAPDDAAIDAVRGQLAQSALLARRATETA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q4KC17 | MKLLHIDSSILGDNSASRQLSHSVVEAWKAAHPATVVTYRDLANDAISHFSAATLVAAGTAAELRDAAQKHEAQLSAQALAEFKAADTVVVAAPMYNFTIPTQLKAWIDRIAVAGETFRYTEAGPQGLCGGKKVIVVSTSGGLHVGQATGVAHEDYLKVLFGFFGITDVEFVRAHGLAYGEEVRSKAMSDAQAQISQQLFAAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q39K00 | MTTILQINSAARSQGAQSTLLANELTAKLQQSNPGAKVVVRDLLADALPHLDESVLGAFFTPADKRTAEQNAIVAKSDALIAELQAADVIVIGAPMYNFGISSQLKTYFDWIARAGVTFRYTENGPEGLIKGKKVHVVTARGGKYAGTPNDSQTPYLRTFLGFVGMTDVNFIFAEGLNLGPDAQSAALAGAREAIAAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q39M92 | MKLLHIDSSILGQGSVSRELSAEVVATFRARDPGLTVTRLDLAATPIGHLSAEHLAAAQGAPISDALKADVEIGQRALAEFLAADIVVIGAPMYNFGIASQLKAWIDRISVAGTTFRYGENGPVGLCGGKKLVVASSRGGVYSEGSPAAAFDHQETYLKAAFGFLGITDITFIRAEGVAMGPDLRSGAIASAKEAAAALAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q39M29 | MPTLLVVEASPRGEQSISRGLTKMFVNQWKREQHDGRVIQRDLMATDLPFVTMPWLGAYFTPPEHQTQDMKNLLRLSDELVAEILSADHIVIGTPVYNYNVPAVLKAYIDHIVRKGKTLGFSGEGLVKGKACTIVMASGGAYTPDSPIRDRDIATGYLRLILKVIGIEDVTVIAGGNAKAVDMGEISRSDFLEAFASDMADAAARPVVQV | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q39M02 | MTRVLYIEGSPNKDYSASIEVCNAFLDTYRHAHPDHEIQKLDIWNLAIPEFDEAALAAKYAGLSGKALTPSQATAWQRIEQLAAPFHEADKFLFGVPLWNFSIPYKLKHLIDAISQKDVLFTFDGAGFAGKLAGKKAAVIYARGLGYQSPGSFTPAAEFDLQRPYMETWLRFVGVQDVTGIVVERTLFGANGTVDRSRAIDEARTIARTF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
C1F513 | MLTLLRLDSSPLETSVSRALTDEFVAAWKAAHPDGVVIVRDLTLAPPPPVDAVWIGACFTPPPQRTAEQNDRLALSDAFLEELERADEYAIGVAMHNFSIPAVLKLWIDQVVRVGRTFAYSDGRPQGLLQGKKATILAATGGVYSAGTPAEGMNFLDPYLKTVLGFLGVRDIQVVTAGGTSQLRNPDVDREAFLEPVLQRVRETAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B9MI46 | MQLLHIDSAITGDQSVSRQLTAQIVEAWKASHPATQVSYLDLVADAPAHFTMDAMAPRTGQTDGLSEAQQRENAVSERLVSQFLAADVVVIGAPFYNFAIPTQLKAWIDRIAQPGRTFQYTANGPEGLAKGKTVIVASSRGGVYSTSEGGRAMEHQESYLQTVLGFFGVTDVRFVRAEGVAMGGDAKAQALAAAAQAIEAHVKAHAANQDRVSQAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
A1W8C6 | MQLLHIDSAITGDQSVSRQLTAQTVEAWKASHPATQVSYLDLVADAPAHFTMDAMAPRTGQTDGLSEAQQRENAVSERLVSQFLAADVVVIGAPFYNFAIPTQLKAWIDRIAQPGRTFQYTANGPEGLAKGKTVIVASSRGGVYSTSEGGRAMEHQESYLQTVLGFFGVTDVRFVRAEGVAMGGDAKAQALAAAAQAIEAHVKAHAANQDRVSQAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
A4SMX2 | MANILVLKSSILGQYSQSNALIDGFLADHQSDTVTVRDLATLNLPVLDGELASGLRGGDNLNERQLAVMAQSDELIAELKGSDLVVIAAPMYNFSIPTQLKNWIDLIARAGVTFRYTETGPVGLVENTRALVISPRGGMHVGSATDLVTPYMRTVLGFIGIKDVDFIYAEGMGMGPDAQAKGIEQAKGQLETLAL | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
C1D6X4 | MKLLHIDSSVLAEHSVSRQLTARIVTEWQATHPGTAVEYLDLAQDTPATLSGAELAARMTPADSRSAEQTAAAARTEAFLQQFLAANVIVVGAPMYNFSIPSQLKNWIDCIAQAGRTFKYTETGPVGLAGNKTVIVASSRGGVYSTSEALRALDHQESYLRTVLGFMGIDNVRIVRAEGVNQGADRRSQALAAAEADIATLV | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q5ZT75 | MKLLAIDSSILTNTSVSRQLTRSFVSRWQKIYPETEVVYRDLHAQPINHLSQKILAANSVPSTQISAEIREEMNLSMQLISELLSASVLVIGAPMYNFSIPSQLKSWIDRIVIAGKTFKYVDGKVQGLATGKRAYILSSRGGFYNAEPALNLDHQERYLTSILNFIGISDITFIRAEGVNVGEEIRTQSLHQAEAKIQQLLQFQMA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B1XW54 | MKILQVNSSARNFANGVGSVSSQLAGELVARLRDGEPTASVVVRDLARTPHPVLDEAALQALFTPADQRTPAQAERVALDDALIAEIQAADVVVIAAPMFNFGITAQLKNWIDAIARAKVTFQYTANGPEGLLKGKRVHVVLTRGGVYRDQASDNQVPYLRQVLGFLGMTDVEFIYAERQGMGPEASAQGVAEAREQIAALLQLGTATA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B9E9A2 | MTKVLYITGHPNDETVSNSMAAGKSFIESYKQSNPDHEVVHIDLYDTFIPLIDKEVFDGWGKLQSGKGFEALSETEQQKVARLNELSDEFAAADKYIFVTPMWNLSFPAVVKAYIDAVAVAGKAFKYTAEGAVGLLTDKKALLIQSRGGIYSEGPAADFELGNRYLQTILGFFGVPSVEELVIEGHNQMPEKAEEIKADGVRRAEALGKTF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q8EWL4 | MAKLLVIKASMVDKSISFSEELTNRFVKYYLESNPNDEVITLDLNEVPMAQKTLNGSNLKNFFNQEDSDFYIDQLKSVHKVIFSCPMTNFNISATAKNYLDHVLVANKTFSYKYSKKGDAIGLLNHLSVQLLTTQGAPLGWYPWGNHTENLKGTFEFMGTKVVTPILVDGTKIPENANKTPVERINEFDSVIRLKAKEFAALPAVDWKPLEQ | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
A6VTC3 | MATLLRIDSSASGENSKSRQLANEFVEKWLAKNPEGKVVARDVTANPLPHFTGETLGALFTPEENRTAEQQAIVAIGDELIAELEAADLVIVSAPMYNFGIPSTLKSYFDHVARAGRTFKYTETGPVGLVNKDAYIFAASGSFLAGAPVDHQVPHIQTFLGFIGLNVKDTFIAGGQAMGEPGEDAFNQAKSQIAVAV | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q600K1 | MNILVIKSSVNEKKGSYSSHLSDLFIKFYLEIHPEDQIEVYDLNQFGLANTNLTIKNFEDKTFYQKAESDFWINKLRKADKIVFSTSMTNFNYSATTKNFFDAITVPNKTFLLDKNTGKYTGLLKNIQNVQILTAQGAPLGWYPFGNHSALIKQIFEFLGAKVRSDFFVLDGTKVAPNNQKPIADFVAQRQNQIKILAENF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q4A7R7 | MNILVIKSSVNEKKGSYSSHLSDLFIKFYLEIHPEDQIEVYDLNQFGLANTNLTMKNFEDKTFYQKAESDFWINKLRNADKIVFSTSMTNFNYSATTKNFFDAITVPNKTFLLDKNTGKYTGLLKNIQNVQILTAQGAPLGWYPFGNHSALIKQIFEFLGAKVRSDFFVLDGTKVAPNNQKPIADFVAQRQNQIKILAENF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q4A9N3 | MNILVIKSSVNEKKGSYSSHLSDLFIKFYLEIHPDDQIEVYDLNQFGLANTNLTMKNFEDKTFYQKAESDFWINKLRNADKIVFSTSMTNFNYSATTKNFFDAITVPNKTFLLDKNTGKYTGLLKNIQNVQILTAQGAPLGWYPFGNHSALIKQIFEFLGANVRSDFFVLDGTKVAPNNQKPIADFVAQRQNQIKILAENF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B3PM20 | MKKVLVLLSSPVAKENSYSTYFATKFVEEYQKINQEDEIKIIDLNSFDVSQKTLTSGNFATFFNENDSDALINELKSVDKLIVASPMINFNVPATLKNYLDHICVANKTFSYKYKAKGASIGLLDHLKVQIITSQGAPSGWYSFSSHTKYLEGLFNFLGIEIAPSIEITGTKVDPKPKEELYLEFEQEIIKKASEF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B7KYE7 | MKLLHVDGSILGPHSVSRTVSAAIVDRLRAQHPGLEVIYRDLAGTPLPHLSGAVLAGAQPNATNTPDVQHDVELGRQVLEEFLAADIVVIGAPLYNFTLSSQLKAWIDRILVAGVTFRYGPTGAEGLAGGKRVIAVVSRGGLYGPGTPAAAAEHAETYLRTVLAFIGITAPEIIVAEGIALGAEARERALAGALDAAAALKAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
A9W4C5 | MKLLHVDGSILGPHSVSRTVSAAIVDRLRAQHPGLDVIYRDLAGTPLPHLSGAVLAGAQPNATNTPDVQHDVELGRQVLEEFLAAEIVVIGAPLYNFTLSSQLKAWIDRILVAGVTFRYGPSGAEGLAGGKRVIAVVSRGGLYGPGTPAAAAEHAETYLRTVLAFIGITAPEVIVAEGIALGPEARERALAGALDAAAALKAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B8IER1 | MKLLHIDTSILGAGSVSRELSALIVERLTRGTQAEVTYRDLAAENLPHLTPATLPSAHPLSAMAGPLDATAQAARAASDRMLEEFIGADTVVVGAPMYNFTIPSQLKAWLDRLAVPGKTFRYGANGPEGLVGGKRVIVAVTRGGFYGRESGAVSAEHAESYLRTILAFMGITEPEFVLAEGLAAGDHNKAQALTSARAAVQQLAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B1ZKG7 | MKLLHVDGSILGPHSVSRTVSAAIVDRLRAQHPDLDVAYRDLAQTPLPHLSGAVLAGAQPNATNAPDVQHDVDLGRQALDEFLAADVVVIGAPLYNFTLSSQLKAWIDRILVAGVTFRYGPSGAEGLAGGKRVIAVVSRGGLYGPGTPAAAAEHAETYLRTVLAFIGITAPEIIVAEGIALGPEARERALAGALDAAAALKAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B1M4X4 | MKLLHLDASILGTGSVSRELSALIVRRLAGDAPDAVTYRDLVAENPPHLTVATLPGAHPVSAMAGPLDAAGQAVRDASDRMLSEFVAADTVVIGVPMYNFTIPSQLKAWIDRLLVPGTTFRYGAAGPEGLMGGKRVILALARGGFYGPGTASVPAEHAEHYLRTVFGFMGIVPELVLAEGLAAGEHNKAQALASARDAVGQLAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
B8EJL7 | MKLLHIDSSILGDHSVSRQLTAAIIARLQEVTPDLDVSHRDLAANPLSHLSGALLAASAPGAPAPDPSTQAALGESAAILAEFLAADIVVVGAPMYNFAISSQLKAWIDRLVIAGKTFRYADGAVEGLAGGRRLIIASSRGGVFEAGAAAAALDYQETYLRAIFGFIGIADVEIIRAEGLAFGEDARALAIKQAGDAILRLEAA | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q2ST93 | MSKVLVLKTTAQADEVSNSVALTNRFLEEYKKFNPDDEIIIVDLNKDEVGTSILTSETFPTFYQQEVTKKYINLLKSVDKLVIACPMYNFSTPVTLKSFIDHVSVANETFSYKYSKKGDAIGLITNLKAQILGVQGAPLGWYPWGQHTQYVEGAMRFLGIEFNKTVLLAGVKVAPLLELTPAQRVETIIDEVIQAAKTF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q7NAW1 | MSKVLFINASPVANEASFSYQLAKTFESEYLKLNPSDQVSWLDLNELDKGSMTLTSKNSKEHFKDENVDPLINQIKSVDKLVVIAPMTNFNYPATLKNWLDKICVANKTFSYKYSKKGGSIGLMDHLKVMIINTQGAPEGWYAFADVTVLLKGVFEFIGAMVDSIKVAGTKVEYLNKQPKEIVEPNLALIKEKAKNF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q49357 | MKKVIIVDASVTPSGSYTHLLLDRFLQTYKKQNSSVEFIDWNLNELPVGKISYNTQNASNFFSFENSDYYIDALKTAYGIVILAPMTNFNYPASLKNFIDHVFVANKTFQDKYVTKGASKGLLTNLKVVVLASQGAPLGWYPWADHVSNLKGLFGFAGVTHFESVLIDDTKILYKDKNKQEVVDLFAHKVDQVANNF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q6KHU1 | MKIQKVLVIKSSMTENLPSGSFSSALSDKFMEYYRKENPIDKIIELNLNDQKDLISLSSQNFNTFFTDGVSDKYIDQLKSVDKVVISSPMTNFNYTALLKNYLDRILVANKTFSYKYSKKGEAIGLLPHLKVQILTTQGAPLGWYTWGDHTKNLEGTFEFIGAKVAKSVVMDGLKTPQYSSLKAPEALDLFDKVIKTAAENF | Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH Binds 1 FMN per subunit. Homodimer. Belongs to the azoreductase type 1 family. |
Q61338 | MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEAERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK | Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles (By similarity). May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). Isoform Bcl-X(S) promotes apoptosis. Homodimer. Interacts with BAD. Interacts with PGAM5. Interacts with HEBP2. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Interacts with ATP5F1A and ATP5F1B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase (By similarity). Interacts with VDAC1 (By similarity). Interacts with BCL2L11 (via BH3) (PubMed:14499110, PubMed:27013495). Interacts with RNF183 (By similarity). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (PubMed:16509771). Interacts with GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and BCL2L1 is impaired in the absence of GIMAP5 (PubMed:21502331). Interacts with isoform 4 of CLU; this interaction releases and activates BAX and promotes cell death (By similarity). Forms heterodimers with BAX, BAK or BCL2; heterodimerization with BAX does not seem to be required for anti-apoptotic activity (By similarity). Interacts with isoform 1 of SIVA1; the interaction inhibits the anti-apoptotic activity (By similarity). Interacts with IKZF3 (By similarity). Interacts with RTL10/BOP (By similarity). Interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF (By similarity). Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts with BECN1 (By similarity). Localizes to the centrosome when phosphorylated at Ser-49. After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. Widely expressed, with highest levels in the brain, thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-TM) expression is enhanced in B- and T-lymphocytes that have been activated. Bcl-X(beta) is expressed in both embryonal and postnatal tissues, whereas Bcl-X(L) is predominantly found in postnatal tissues. The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death. The loop between motifs BH4 and BH3 is required for the interaction with NLRP1. Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity. Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity). Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome. Belongs to the Bcl-2 family. |
O77737 | MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK | Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). Homodimer. Heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Interacts with BCL2L11. Interacts with BAD. Interacts with SIVA1 isoform 1; the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. Interacts with IKZF3. Interacts with HEBP2. Interacts with BOP. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Interacts with DNM1L and CLTA; DNM1L and BCL2L1 may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with ATP5F1A and ATP5F1B; the interactions mediate the association of BCL2L1 with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase. Interacts with VDAC1. Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV. Interacts with BCL2L11 (via BH3) (By similarity). Interacts with RNF183 (By similarity). Interacts with GIMAP3/IAN4 (By similarity). Interacts with GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and BCL2L1 is impaired in the absence of GIMAP5 (By similarity). Interacts with CLU (isoform 4); this interaction releases and activates BAX and promotes cell death (By similarity). After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. Localizes to the centrosome when phosphorylated at Ser-49 (By similarity). The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death. The loop between motifs BH4 and BH3 is required for the interaction with NLRP1. Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity. Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity). Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome. Belongs to the Bcl-2 family. |
Q64128 | MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK | Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). Isoform Bcl-X(S) promotes apoptosis. Homodimer. Interacts with BCL2L11 (By similarity). Interacts with BAD. Interacts with PGAM5. Interacts with HEBP2. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Interacts with ATP5F1A and ATP5F1B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase (PubMed:21926988). Interacts with VDAC1 (By similarity). Interacts with BCL2L11 (via BH3) (By similarity). Interacts with RNF183 (By similarity). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (By similarity). Interacts with GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and BCL2L1 is impaired in the absence of GIMAP5 (By similarity). Interacts with isoform 4 of CLU; this interaction releases and activates BAX and promotes cell death (By similarity). Forms heterodimers with BAX, BAK or BCL2; heterodimerization with BAX does not seem to be required for anti-apoptotic activity (By similarity). Interacts with isoform 1 of SIVA1; the interaction inhibits the anti-apoptotic activity (By similarity). Interacts with IKZF3 (By similarity). Interacts with RTL10/BOP (By similarity). Interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF (PubMed:18250306, PubMed:23792689). Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts with BECN1 (By similarity). Localizes to the centrosome when phosphorylated at Ser-49 (By similarity). After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. Expressed in most tissues. Bcl-X(beta) is specifically expressed in cerebellum, heart, and thymus. In the ovary, the predominant form is Bcl-X(L), with a small but detectable level of Bcl-X(S). The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death. The loop between motifs BH4 and BH3 is required for the interaction with NLRP1. Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity (By similarity). Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity). Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome. Belongs to the Bcl-2 family. Extended N-terminus. Extended N-terminus. |
Q1RMX3 | MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK | Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX (By similarity). Interacts with HIF3A (via C-terminus domain). Interacts with BOP. Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane (By similarity). The BH4 motif seems to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2 (By similarity). Belongs to the Bcl-2 family. |
Q45T69 | MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK | Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX (By similarity). Interacts with HIF3A (via C-terminus domain). Interacts with BOP. Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane (By similarity). The BH4 motif seems to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2 (By similarity). Belongs to the Bcl-2 family. |
Q5U0H4 | MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETQLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK | Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. Interacts with HIF3A (via C-terminus domain). Interacts with BOP. Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane. Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines. The BH4 motif seems to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2. Based on a readthrough transcript which may produce a BCL2L2-PABPN1 fusion protein. Belongs to the Bcl-2 family. Extended N-terminus. |
Q9CYW5 | MATPASTPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQDWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK | Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. Interacts with HIF3A isoform 2 (via C-terminus domain) (PubMed:21546903). Interacts with BOP (By similarity). Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane (By similarity). Expressed in almost all myeloid cell lines and in a wide range of tissues, with highest levels in brain, colon, and salivary gland. Expressed in both mitotic and postmitotic Sertoli cells. By Igf1. The BH4 motif seems to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2 (By similarity). Mice are sterile due to arrest in spermatogenesis associated with a gradual loss of germ and Sertoli cells from the testis. Belongs to the Bcl-2 family. |
P86042 | GLFSVVTGVLKAVGKNVAGSLLEQLKCKISGGC | Antimicrobial peptide. Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
P0C5X1 | GLLSAVKGVLKGAGKNVAGSLMDKLKCKLFGGC | Antimicrobial peptide. Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
P0C5X2 | GLFDVVKGVLKGAGKNVAGSLLEQLKCKLSGGC | Antimicrobial peptide. Active against the Gram-positive bacterium S.aureus (MIC=30 uM) and the Gram-negative bacterium E.coli (MIC=30 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
P0C5X3 | GLFDVVKGVLKGVGKNVAGSLLEQLKCKLSGGC | Antimicrobial peptide. A mixture of Brevinin-2DYc/2DYd is active against the Gram-positive bacterium S.aureus (MIC=15 uM) and the Gram-negative bacterium E.coli (MIC=15 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
P0C5X4 | GIFDVVKGVLKGVGKNVAGSLLEQLKCKLSGGC | Antimicrobial peptide. A mixture of Brevinin-2DYc/2DYd is active against the Gram-positive bacterium S.aureus (MIC=15 uM) and the Gram-negative bacterium E.coli (MIC=15 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
P0C5X5 | GLFSVVTGVLKAVGKNVAKNVGGSLLEQLKCKISGGC | Antimicrobial peptide. Active against the Gram-positive bacterium S.aureus (MIC=15 uM) and the Gram-negative bacterium E.coli (MIC=30 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
C0HL69 | GLLDTPKNLALNAAKSAGVSVLNSLSCKLSKTC | Antimicrobial peptide active against the Gram-positive bacterium S.aureus (MIC=50 uM) and against the Gram-negative bacteria E.coli (MIC=12.5 uM). Has no antifungal activity against C.albicans. Shows hemolytic activity against human erythrocytes only at high concentrations (LC(50)=140 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
C0HL70 | GVLGTVKNLLIGAGKSAAQSVLKTLSCKLSNDC | Antimicrobial peptide active against the Gram-positive bacterium S.aureus (MIC=25 uM) and against the Gram-negative bacteria E.coli (MIC=6 uM). Has no antifungal activity against C.albicans. Shows hemolytic activity against human erythrocytes only at high concentrations (LC(50)=180 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
C0HL71 | GLFTLIKGAAKLIGKTVAKEAGKTGLELMACKITNQC | Antimicrobial peptide active against the Gram-positive bacterium S.aureus (MIC=50 uM) and against the Gram-negative bacteria E.coli (MIC=12.5 uM). Has no antifungal activity against C.albicans. Shows hemolytic activity against human erythrocytes only at high concentrations (LC(50)=100 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
E7EKE0 | MFTLKKPLLLLFFLGTISLSLCQEERDADEEEGEMIEEEVKRSLLGTVKDLLIGAGKSAAQSVLKGLSCKLSKDC | Has antimicrobial activity against some Gram-positive bacteria and fungi but has no activity against a range of Gram-negative bacteria except P.faecalis. Has antimicrobial activity against the Gram-positive bacteria S.aureus ATCC 25923 (MIC=19 uM), B.licheniformis X39 (MIC=37.5 uM) and R.rhodochrous X15 (MIC=9.5 uM), is virtually inactive against E.faecium 091299 (MIC=150 uM) and S.carnosus KHS (MIC=150 uM) and inactive against E.faecalis 981. Active against the Gram-negative bacterium P.faecalis X29 (MIC=9.5 uM) and is inactive against E.coli, P.aeruginosa and S.typhi. Active against C.albicans ATCC 2002 (MIC=19 uM) and is also active against the slime mold 090223 (MIC=37.5 uM). Has extremely low hemolytic activity against human erythrocytes (LC(50)=300 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
E7EKE1 | MFTMKKPLLLIVLLGIISLSLCEQERAADEEEGEMIEEEVKRSLLGTVKDLLIGAGKSAAQSVLKGLSCKLSKDC | Has antimicrobial activity against some Gram-positive bacteria and fungi but has no activity against a range of Gram-negative bacteria except P.faecalis. Has antimicrobial activity against the Gram-positive bacteria S.aureus ATCC 25923 (MIC=19 uM), B.licheniformis X39 (MIC=37.5 uM) and R.rhodochrous X15 (MIC=9.5 uM), is virtually inactive against E.faecium 091299 (MIC=150 uM) and S.carnosus KHS (MIC=150 uM) and inactive against E.faecalis 981. Active against the Gram-negative bacterium P.faecalis X29 (MIC=9.5 uM) and is inactive against E.coli, P.aeruginosa and S.typhi. Active against C.albicans ATCC 2002 (MIC=19 uM) and is also active against the slime mold 090223 (MIC=37.5 uM). Has extremely low hemolytic activity against human erythrocytes (LC(50)=300 uM). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. |
C0JB68 | WIMGHMVNPFEQVDEFLNLGANAIEFDIDFDENGIAKYTHHGIPCDCGRLCTKSAVFTEYLDYVRQVTSPGDPKFRKELVLLALDLKLQRISSEKAYAAGVDVATKLLDHYWKRGWNGGRAYILLNIPLVEDYEFIKGFKDTLRKEGHEQYNAKVGINFTGNEDLDEIRKVLEKLGEDEHIWQADGITSCFARGTDRLEKALEKRDTPGYKYISKVYAWTLVRSSIMRRSLRLGVDGVMSNNPDRVVKVLKEKEFANKFRLATYADNPWEKFTPI | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
C0JB67 | WIMGHMVNSIEQVDKFLDLGANAIEFDVDFDDDGVAKYTHHGIPCDCGRLCNKYAVFTEYLDYVRQVTTPGDPKFRKELVLLALDLKLQRISSEKAYAAGVDVATKLLDHYWMRGKNGGRAYILLNIPLVKHYEFIRAFKDTLRKEGHEQYNAKVGINFTGNEDLDEIRKVLEKLGEDEHIWQADGIASCIPRGTERLKKVLEKRDTPGYKYISKVYAWTLVRSSIMRRSLSLGVDGVMSNYPDIVVKVLKEKKFSDKFRLATYADNPWEKFTPI | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
Q09200 | MRLDRRALYALVLLLACASLGLLYSSTRNAPSLPNPLALWSPPQGPPRLDLLDLAPEPRYAHIPVRIKEQVVGLLAQNNCSCESKGGSLPLPFLRQVRAVDLTKAFDAEELRAVSVAREQEYQAFLARSRSLADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQEASVQEIYQVNLSASLGTWDVAGEVTGVTLTGEGQPDLTLASPVLDKLNRQLQLVTYSSRSYQANTADTVRFSTKGHEVAFTILVRHPPNPRLYPPSSLPQGAEYNISALVTIATKTFLRYDRLRTLIASIRRFYPTVTIVIADDSDKPERISDPHVEHYFMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFVFTARTRLEKLVDVLEKTPLDLVGGAVREISGYATTYRQLLSVEPGAPGLGNCFRQKQGFHHELVGFPSCVVTDGVVNFFLARTDKVRQVGFDPRLNRVAHLEFFLDGLGFLRVGSCSDVVVDHASKVKLPWTAKDPGAETYARYRYPGSLDQSQVAKHRLLFFKHRLQCMTAE | Involved in the biosynthesis of gangliosides GM2, GD2 and GA2. Involved in the biosynthesis of gangliosides GM2, GD2, GT2 and GA2 from GM3, GD3, GT3 and GA3, respectively. ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GM2 (d18:1(4E)) + H(+) + UDP ganglioside GD3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GD2 (d18:1(4E)) + H(+) + UDP ganglioside GM3 + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GM2 + H(+) + UDP ganglioside GD3 + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GD2 + H(+) + UDP ganglioside GD1a + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GalNAc-GD1a + H(+) + UDP ganglioside GT3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GT2 (d18:1(4E)) + H(+) + UDP a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GA2 (d18:1(4E)) + H(+) + UDP alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-beta-D-galactosaminyl-(1->4)-[alpha-N-glycoloylneuraminosyl-(2->3)]-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + UDP Sphingolipid metabolism. Homodimer; disulfide-linked. Most abundant in brain, liver, lung, spleen and testis. Highest at day 7 of embryonic development after which it declines to its lowest levels at day 11 before increasing again. No visible phenotype, excepting a slight decrease in neural conduction velocity from the tibial nerve to the somatosensory cortex (PubMed:8855236). Mutant mice display impaired motor coordination and balance (PubMed:15953602). Sciatic nerves from over three month old mutant mice show signs of Wallerian degeneration, with redundant myelin, degeneration of myelinated fibers, axon dysmyelination, and an apparent decrease in the diameter of myelinated axons (PubMed:15953602). The distances between neurofilaments in myelinated axons from over 3 month old mice are shorter than normal (PubMed:15953602). Mice are less sensitive to C.botulinum neurotoxin type C (BoNT/C), C.botulinum neurotoxin type D (BoNT/D, botD) and C.botulinum neurotoxin type F (BoNT/F, botF) (PubMed:21483489). Belongs to the glycosyltransferase 2 family. Beta-1,4 N-acetylgalactosaminyltransferase 1 |
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