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CAZyme Information: AMAG_11933-t26_1-p1

You are here: Home > Sequence: AMAG_11933-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Allomyces macrogynus
Lineage Blastocladiomycota; Blastocladiomycetes; ; Blastocladiaceae; Allomyces; Allomyces macrogynus
CAZyme ID AMAG_11933-t26_1-p1
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
168 19021.77 8.0056
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AmacrogynusATCC38327 19333 578462 535 18798
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in AMAG_11933-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 1 161 1e-34 0.611764705882353

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 3.04e-80 1 164 105 253
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 6.08e-54 2 162 107 245
L-ascorbate peroxidase
178467 PLN02879 9.62e-45 2 160 110 246
L-ascorbate peroxidase
166005 PLN02364 4.99e-44 2 160 109 246
L-ascorbate peroxidase 1
173823 plant_peroxidase_like 1.20e-35 1 158 99 255
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.95e-69 1 163 105 270
8.18e-69 1 163 105 270
3.91e-68 1 163 117 281
3.91e-68 1 163 117 281
3.91e-68 1 163 117 281

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.93e-47 1 162 102 260
Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
5.27e-47 1 162 102 260
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
5.56e-47 1 162 102 260
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]
5.71e-47 1 162 103 261
The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
1.81e-45 1 162 103 261
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.84e-68 1 163 105 270
Putative heme-binding peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP2 PE=3 SV=1
1.02e-65 1 163 117 281
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
1.08e-65 1 163 104 263
Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1
2.15e-64 1 161 194 350
Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1
2.72e-64 1 163 105 271
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000038 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in AMAG_11933-t26_1-p1.