Species | Candida albicans | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida albicans | |||||||||||
CAZyme ID | C5_00810C_A-T-p1 | |||||||||||
CAZy Family | GT20 | |||||||||||
CAZyme Description | Putative heme-binding peroxidase [Source:UniProtKB/Swiss-Prot;Acc:Q59X94] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA2 | 33 | 285 | 5.3e-60 | 0.9764705882352941 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 3.44e-126 | 30 | 289 | 13 | 253 | Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water. |
178218 | PLN02608 | 5.21e-68 | 50 | 287 | 29 | 245 | L-ascorbate peroxidase |
178467 | PLN02879 | 5.49e-62 | 52 | 285 | 34 | 246 | L-ascorbate peroxidase |
173823 | plant_peroxidase_like | 2.60e-61 | 35 | 283 | 1 | 255 | Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase. |
223453 | KatG | 4.36e-58 | 47 | 286 | 90 | 417 | Catalase (peroxidase I) [Inorganic ion transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
4.77e-95 | 30 | 288 | 6 | 263 | |
9.46e-94 | 30 | 286 | 88 | 346 | |
7.94e-92 | 30 | 290 | 19 | 283 | |
7.94e-92 | 30 | 290 | 19 | 283 | |
7.94e-92 | 30 | 290 | 19 | 283 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.16e-75 | 51 | 287 | 25 | 260 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
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8.19e-75 | 51 | 287 | 25 | 260 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
8.72e-75 | 51 | 287 | 25 | 260 | Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major] |
|
9.00e-75 | 51 | 287 | 26 | 261 | The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin] |
|
2.91e-73 | 51 | 287 | 26 | 261 | The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.78e-213 | 1 | 291 | 1 | 291 | Putative heme-binding peroxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CCP2 PE=3 SV=2 |
|
1.05e-132 | 31 | 290 | 158 | 417 | Putative heme-binding peroxidase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=DEHA2G12166g PE=3 SV=3 |
|
8.47e-96 | 30 | 288 | 6 | 263 | Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1 |
|
1.05e-89 | 30 | 290 | 19 | 283 | Putative heme-binding peroxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FGRRES_10606 PE=3 SV=1 |
|
9.35e-88 | 30 | 285 | 40 | 296 | Putative heme-binding peroxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D25366g PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.745399 | 0.254604 |
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