Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna25391.1-v1.0-hybrid |
Family | AA2 |
Protein Properties | Length: 677 Molecular Weight: 76082.4 Isoelectric Point: 5.0799 |
Chromosome | Chromosome/Scaffold: 3 Start: 19265955 End: 19271166 |
Description | ascorbate peroxidase 1 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 451 | 672 | 0 |
GLIAEKNCAPLMLRLAWHSAGTYDVKTKTGGPFGTMKQPAELAHGANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPDVPFHPGREDKPE PPPEGRLPDAGKGSDHLREVFGKTMGLSDQDIVALSGGHTLGRAHKERSGFEGPWTPNPLIFDNSYFTVLLSGEKEGLLQLPTDKALLSDPVFRPLVEKY AADEDAFFADYALAHQRLSELG |
Full Sequence |
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Protein Sequence Length: 677 Download |
MSDYIPEDVV NKILLKLPIK SLMRCRVVCH SWNNLIKSST FINSHLCSIS QLHSENEAHD 60 LLLLQGYADE NGPVIYSLHW DDPELSECTD FITPTYTIVP DLIGTCNGLV CLSTCSSLSA 120 GRIILWNPSI RKYVFSSIPS SCFDGEENFA FGYNSNNNDY KVLLLTDRQA EDDQTVHAGM 180 VWPFASGDWK SFSHETLEPI DVYSPFEEGL ASVNKVLHWL QYELTEDYDD KYIVSIVSFD 240 LVTDSFKLQE AWVNKTLSSI RITRYEETLA VFEFRSYENE EFVDMWVMKE YGENCWTKLV 300 TLRHGLSIDP FGFKNSREIV VGVEDEEGRL ELKSMNMDGK QVKQFGRSGY KFFFMDSFIE 360 SLPALVEVRP LTRETWLRRT KKLNKKEKWA RSDMDLCSTR ASASSIARVL TSHFSLISSA 420 SQGLLTMGKC YPTVSEEYKK AIDKAKRKLR GLIAEKNCAP LMLRLAWHSA GTYDVKTKTG 480 GPFGTMKQPA ELAHGANNGL DIAVRLLEPI KEQFPILSYA DFYQLAGVVA VEVTGGPDVP 540 FHPGREDKPE PPPEGRLPDA GKGSDHLREV FGKTMGLSDQ DIVALSGGHT LGRAHKERSG 600 FEGPWTPNPL IFDNSYFTVL LSGEKEGLLQ LPTDKALLSD PVFRPLVEKY AADEDAFFAD 660 YALAHQRLSE LGFAEA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 2.0e-49 | 443 | 649 | 235 | + 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. | ||
PLN02608 | PLN02608 | 5.0e-131 | 432 | 673 | 242 | + L-ascorbate peroxidase | ||
PLN02879 | PLN02879 | 7.0e-134 | 427 | 675 | 249 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 3.0e-135 | 427 | 676 | 250 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 3.0e-137 | 431 | 676 | 254 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004601 | peroxidase activity |
GO:0005515 | protein binding |
GO:0006979 | response to oxidative stress |
GO:0020037 | heme binding |
GO:0055114 | oxidation-reduction process |
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 | 428 | 676 | 1 | 249 | A Chain A, Polygalacturonase From Aspergillus Aculeatus |
PDB | 2xih_A | 0 | 428 | 676 | 1 | 249 | A Chain A, Polygalacturonase From Aspergillus Aculeatus |
PDB | 2xif_A | 0 | 428 | 676 | 1 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 428 | 676 | 1 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2y6b_A | 0 | 428 | 676 | 1 | 249 | A Chain A, Ascorbate Peroxidase R38k Mutant |
Sequence Alignments (This image is cropped. Click for full image.) |
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