y
Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb05g009400.1 |
Family | AA2 |
Protein Properties | Length: 342 Molecular Weight: 35827.7 Isoelectric Point: 6.1283 |
Chromosome | Chromosome/Scaffold: 5 Start: 18669834 End: 18671112 |
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 | 59 | 323 | 9.30042e-42 |
GSADPTILPALIRLQFHDCFVRGCDASVLIKGGAGGNNAEVDNSKHQGLRGVEIIEGAKTQLEALCPGVVSCADIVVLAARDAISFTGGPSFDVPTGRLD GKVSNLRDADALPDVHDGIDALRSKFRANGLDEKDLVLLTAAHTVGTTACFFLQDRLYNFPLPGGGRGSDPTIPPGFLSELKSRCAPGDLNTRLALDRGS EGVFDTSILRNIRNGFAVIGSDAALYNDTATVDVVDSYSGLLSNFFGPYFRQDFADAMVRMGSIG |
Full Sequence |
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Protein Sequence Length: 342 Download |
MATRRCSSSN VPPAGLLAVP CLLLLLLAGV SNGQLQVGFY SNSCPGAEST VASVVRQSGS 60 ADPTILPALI RLQFHDCFVR GCDASVLIKG GAGGNNAEVD NSKHQGLRGV EIIEGAKTQL 120 EALCPGVVSC ADIVVLAARD AISFTGGPSF DVPTGRLDGK VSNLRDADAL PDVHDGIDAL 180 RSKFRANGLD EKDLVLLTAA HTVGTTACFF LQDRLYNFPL PGGGRGSDPT IPPGFLSELK 240 SRCAPGDLNT RLALDRGSEG VFDTSILRNI RNGFAVIGSD AALYNDTATV DVVDSYSGLL 300 SNFFGPYFRQ DFADAMVRMG SIGVVTGRKQ GEVRKVCSKF N* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 3.0e-11 | 67 | 204 | 144 | + 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 | 2.0e-16 | 49 | 321 | 300 | + 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 | 1.0e-53 | 51 | 203 | 154 | + Peroxidase. | ||
PLN03030 | PLN03030 | 1.0e-96 | 36 | 341 | 307 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 2.0e-136 | 34 | 340 | 308 | + 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 | ABA92027.1 | 0 | 31 | 341 | 15 | 322 | Peroxidase 43 precursor, putative, expressed [Oryza sativa (japonica cultivar-group)] |
GenBank | ACM17566.1 | 0 | 32 | 341 | 26 | 332 | peroxidase [Oryza glaberrima] |
GenBank | ACM17578.1 | 0 | 32 | 341 | 28 | 335 | peroxidase [Oryza granulata] |
GenBank | ACM17593.1 | 0 | 32 | 341 | 26 | 332 | peroxidase [Oryza sativa Indica Group] |
RefSeq | XP_002449395.1 | 0 | 1 | 341 | 1 | 341 | hypothetical protein SORBIDRAFT_05g009400 [Sorghum bicolor] |
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 | 34 | 341 | 2 | 304 | A Chain A, Pyrobaculum Calidifontis Esterase Monoclinic Form |
PDB | 1pa2_A | 0 | 34 | 341 | 2 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 3hdl_A | 0 | 35 | 341 | 2 | 303 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 1qgj_B | 0 | 34 | 341 | 1 | 299 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 1qgj_A | 0 | 34 | 341 | 1 | 299 | A Chain A, Arabidopsis Thaliana Peroxidase N |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |