Species | Mucor circinelloides | |||||||||||
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Lineage | Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides | |||||||||||
CAZyme ID | HMPREF1544_11634-t46_1-p1 | |||||||||||
CAZy Family | GT62 | |||||||||||
CAZyme Description | cytochrome c peroxidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA2 | 13 | 266 | 6.1e-62 | 0.984313725490196 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 9.91e-126 | 8 | 266 | 10 | 250 | 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 | 1.94e-83 | 33 | 270 | 31 | 248 | L-ascorbate peroxidase |
178467 | PLN02879 | 3.73e-66 | 11 | 269 | 6 | 250 | L-ascorbate peroxidase |
166005 | PLN02364 | 8.06e-66 | 33 | 265 | 33 | 246 | L-ascorbate peroxidase 1 |
173823 | plant_peroxidase_like | 1.13e-57 | 13 | 263 | 2 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.80e-109 | 14 | 266 | 10 | 268 | |
6.85e-109 | 4 | 266 | 81 | 346 | |
7.03e-109 | 14 | 266 | 10 | 268 | |
3.00e-108 | 11 | 268 | 6 | 263 | |
3.12e-107 | 6 | 271 | 2 | 274 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.81e-71 | 34 | 271 | 27 | 264 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
|
1.58e-70 | 3 | 271 | 1 | 265 | The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin] |
|
2.03e-70 | 34 | 271 | 27 | 264 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
3.06e-70 | 34 | 271 | 27 | 264 | 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] |
|
3.18e-70 | 24 | 266 | 33 | 274 | Chain A, Cytochrome C Peroxidase [Saccharomyces cerevisiae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.74e-112 | 11 | 266 | 7 | 268 | Putative heme-binding peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP2 PE=3 SV=1 |
|
5.34e-109 | 11 | 268 | 6 | 263 | Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1 |
|
1.53e-107 | 6 | 268 | 2 | 271 | Putative heme-binding peroxidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN5440 PE=3 SV=1 |
|
2.33e-103 | 2 | 272 | 79 | 351 | Cytochrome c peroxidase, mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ccp1 PE=3 SV=1 |
|
1.07e-102 | 6 | 268 | 2 | 271 | Putative heme-binding peroxidase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=AFUA_6G13570 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000062 | 0.000000 |
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