y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s112_99V6.1 |
Family | AA2 |
Protein Properties | Length: 328 Molecular Weight: 35268.5 Isoelectric Point: 9.2421 |
Chromosome | Chromosome/Scaffold: 112 Start: 583450 End: 584974 |
Description | Peroxidase superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 54 | 308 | 0 |
FSRDQSITPALLRLFFHDCFVTGCDASLLINSTPTNSAEKDAGANLTVRGFDLIDTAKAAVERVCPGMVSCADIIALATRDAVRLSGGPNFAMPTGRRDG RVSRADNVNLPGPTVSVADATRIFNAQGLTRNDMVTLLGAHSVGITHCSFFHERLWNFEGTGSADPSMDPNLVMRLKAICPQQGVGLGSPVNLDQATPNI MDNTFYNQLIARKGILQLDQRVATDRTTTARVNVLASPRSTFTAAFAASLIRLGN |
Full Sequence |
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Protein Sequence Length: 328 Download |
MAEQRLRGGA WGVVLLLVRL MSLLHGTKAL RVGFYNNICP GTETIVRQVV ENRFSRDQSI 60 TPALLRLFFH DCFVTGCDAS LLINSTPTNS AEKDAGANLT VRGFDLIDTA KAAVERVCPG 120 MVSCADIIAL ATRDAVRLSG GPNFAMPTGR RDGRVSRADN VNLPGPTVSV ADATRIFNAQ 180 GLTRNDMVTL LGAHSVGITH CSFFHERLWN FEGTGSADPS MDPNLVMRLK AICPQQGVGL 240 GSPVNLDQAT PNIMDNTFYN QLIARKGILQ LDQRVATDRT TTARVNVLAS PRSTFTAAFA 300 ASLIRLGNVR VIEGSGGEIR KICSRIN* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 1.0e-9 | 56 | 200 | 154 | + 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. | ||
cd00314 | plant_peroxidase_like | 3.0e-16 | 46 | 210 | 184 | + 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. | ||
pfam00141 | peroxidase | 2.0e-62 | 46 | 196 | 153 | + Peroxidase. | ||
PLN03030 | PLN03030 | 3.0e-93 | 31 | 327 | 303 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 1.0e-150 | 30 | 326 | 298 | + Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites. |
Gene Ontology | |
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GO Term | Description |
GO:0004601 | peroxidase activity |
GO:0006979 | response to oxidative stress |
GO:0020037 | heme binding |
GO:0055114 | oxidation-reduction process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABN08467.1 | 0 | 30 | 327 | 20 | 312 | Haem peroxidase, plant/fungal/bacterial [Medicago truncatula] |
RefSeq | XP_001759079.1 | 0 | 21 | 327 | 1 | 307 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769260.1 | 0 | 21 | 327 | 1 | 307 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002319196.1 | 0 | 30 | 327 | 23 | 311 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002525672.1 | 0 | 30 | 327 | 21 | 312 | Peroxidase 44 precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1qo4_A | 0 | 30 | 327 | 3 | 304 | A Chain A, Recombinant Horseradish Peroxidase C1a Ala170gln |
PDB | 1pa2_A | 0 | 30 | 327 | 3 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 4a5g_B | 0 | 29 | 327 | 3 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 4a5g_A | 0 | 29 | 327 | 3 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3hdl_A | 0 | 30 | 327 | 2 | 303 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |