Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 119039 |
Family | AA2 |
Protein Properties | Length: 287 Molecular Weight: 31718.9 Isoelectric Point: 4.9777 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 20 | 245 | 0 |
RQELRGMIVEKQCAPIMLRLAWHDAGTYDRETKTGGPNGSIRLEGEYNHIANRGIKAAIDLCEEIKEKCPKISYADLYQLAGVTAVEVTGGPTISFVSGR KDSSVIPPEGRLPDASQGANHLRDVFGRMGLNDKDIVALSGGHTLGRAHKDRSGFDGPWTSNPLIFDNSYFIELIEGEKTGLLKLPTDTCLMEDKVFRQY VETYAKDKDTFFRDYAWSHKKLSELG |
Full Sequence |
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Protein Sequence Length: 287 Download |
MAAEVPLVDH EYVMEIEKAR QELRGMIVEK QCAPIMLRLA WHDAGTYDRE TKTGGPNGSI 60 RLEGEYNHIA NRGIKAAIDL CEEIKEKCPK ISYADLYQLA GVTAVEVTGG PTISFVSGRK 120 DSSVIPPEGR LPDASQGANH LRDVFGRMGL NDKDIVALSG GHTLGRAHKD RSGFDGPWTS 180 NPLIFDNSYF IELIEGEKTG LLKLPTDTCL MEDKVFRQYV ETYAKDKDTF FRDYAWSHKK 240 LSELGFIDHP DETQENTYDS SFTSITILIG VVITAAAVGL VAMIWS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 4.0e-56 | 17 | 243 | 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. | ||
PLN02364 | PLN02364 | 4.0e-111 | 1 | 247 | 248 | + L-ascorbate peroxidase 1 | ||
PLN02879 | PLN02879 | 9.0e-113 | 6 | 248 | 243 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 4.0e-151 | 11 | 246 | 243 | + 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. | ||
PLN02608 | PLN02608 | 3.0e-167 | 1 | 281 | 281 | + L-ascorbate peroxidase |
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 | 2xj6_A | 0 | 6 | 248 | 5 | 248 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 2xih_A | 0 | 6 | 248 | 5 | 248 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 2xif_A | 0 | 6 | 248 | 5 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 6 | 248 | 5 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 1apx_D | 0 | 6 | 248 | 5 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
ascorbate glutathione cycle | RXN-3521 | - | L-ascorbate peroxidase |
L-ascorbate degradation III | RXN-12440 | EC-1.11.1.11 | L-ascorbate peroxidase |
L-ascorbate degradation V | RXN-12440 | EC-1.11.1.11 | L-ascorbate peroxidase |