Species | Rhizopus microsporus | |||||||||||
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Lineage | Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus microsporus | |||||||||||
CAZyme ID | ORE08107.1 | |||||||||||
CAZy Family | GT15 | |||||||||||
CAZyme Description | L-ascorbate oxidase [Source:UniProtKB/TrEMBL;Acc:A0A1X0R7S1] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA1 | 35 | 517 | 6.8e-71 | 0.9106145251396648 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
274555 | ascorbase | 7.52e-66 | 14 | 519 | 1 | 497 | L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. |
132431 | ascorbOXfungal | 1.73e-64 | 35 | 517 | 28 | 503 | L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. |
215324 | PLN02604 | 2.48e-58 | 10 | 519 | 20 | 520 | oxidoreductase |
177843 | PLN02191 | 8.52e-55 | 1 | 517 | 10 | 518 | L-ascorbate oxidase |
259868 | CuRO_2_LCC_like | 3.47e-41 | 166 | 318 | 1 | 152 | Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.99e-131 | 13 | 521 | 26 | 544 | |
9.75e-119 | 15 | 518 | 26 | 613 | |
1.67e-102 | 11 | 523 | 19 | 525 | |
4.72e-95 | 17 | 519 | 18 | 539 | |
1.28e-59 | 27 | 522 | 43 | 492 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.88e-46 | 15 | 519 | 4 | 497 | Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo] |
|
2.64e-33 | 33 | 494 | 20 | 437 | Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae] |
|
5.89e-29 | 18 | 495 | 7 | 425 | Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta] |
|
8.91e-29 | 37 | 521 | 24 | 506 | Crystal Structure of the Zea Mays laccase 3 [Zea mays],6KLI_A Crystal Structure of the Zea Mays laccase 3 complexed with sinapyl [Zea mays],6KLJ_A Crystal Structure of the Zea Mays laccase 3 complexed with coniferyl [Zea mays] |
|
1.08e-28 | 18 | 495 | 7 | 425 | Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.67e-46 | 15 | 519 | 4 | 497 | L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1 |
|
3.50e-44 | 15 | 519 | 34 | 527 | L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2 |
|
3.90e-44 | 13 | 519 | 37 | 533 | L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1 |
|
4.11e-43 | 28 | 516 | 37 | 514 | L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1 |
|
8.28e-43 | 12 | 516 | 28 | 521 | L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000067 | 0.000010 |
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