Species | Rhizopus microsporus | |||||||||||
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Lineage | Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus microsporus | |||||||||||
CAZyme ID | ORE09557.1 | |||||||||||
CAZy Family | GT31 | |||||||||||
CAZyme Description | L-ascorbate oxidase [Source:UniProtKB/TrEMBL;Acc:A0A1X0RBZ2] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA1 | 40 | 533 | 4.9e-88 | 0.9664804469273743 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
274555 | ascorbase | 1.36e-92 | 19 | 547 | 2 | 530 | 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. |
177843 | PLN02191 | 1.27e-80 | 4 | 547 | 9 | 553 | L-ascorbate oxidase |
215324 | PLN02604 | 8.75e-80 | 4 | 547 | 10 | 553 | oxidoreductase |
132431 | ascorbOXfungal | 2.50e-76 | 23 | 533 | 13 | 524 | 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. |
274556 | laccase | 3.15e-54 | 16 | 538 | 1 | 518 | laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.29e-168 | 18 | 551 | 25 | 651 | |
9.89e-143 | 4 | 545 | 6 | 573 | |
3.37e-133 | 21 | 546 | 18 | 571 | |
8.14e-108 | 4 | 511 | 6 | 518 | |
4.81e-75 | 13 | 547 | 28 | 558 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.10e-64 | 18 | 547 | 3 | 530 | 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] |
|
2.10e-52 | 37 | 542 | 20 | 481 | 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] |
|
5.99e-40 | 22 | 546 | 7 | 479 | Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2] |
|
1.22e-39 | 19 | 546 | 68 | 548 | Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada] |
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1.66e-39 | 19 | 546 | 68 | 548 | Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.78e-68 | 16 | 547 | 18 | 549 | L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1 |
|
6.43e-68 | 16 | 547 | 28 | 557 | L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1 |
|
3.20e-65 | 16 | 550 | 21 | 553 | L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1 |
|
4.17e-63 | 18 | 547 | 3 | 530 | L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1 |
|
1.41e-62 | 18 | 547 | 33 | 560 | L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000716 | 0.999255 | CS pos: 16-17. Pr: 0.9694 |
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