y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si029563m |
Family | AA2 |
Protein Properties | Length: 507 Molecular Weight: 52388.5 Isoelectric Point: 4.8079 |
Chromosome | Chromosome/Scaffold: 2 Start: 46728144 End: 46730113 |
Description | Peroxidase superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 238 | 485 | 0 |
GTGAGLIRLFFHDCFVEGCDASVLLNTTGSTRPTERASVPNLSLRGFEVIDAAKAALEAACPGVVSCADIVAFAGRDATFFLSGNAVDFDMPAGRYDGHV SLDSAAIANLPPPFASLKELKDMFAAKGLDTEDMVTLSGAHTVGRSQCSSFSDRLPPNASDMNATLAASLTSQCNGTGDPTVPQDFVTPSGLDSQYYRNV LNHEVLFGSDAALLASDQTAGMVRDNAFKPGLWEDKFKAAMVKMGRAG |
Full Sequence |
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Protein Sequence Length: 507 Download |
MAKLAVPITL LLALLGSPEP VELDSTYESS SQSTELTCLS SQPNPPIYPP SSSPSSSTPP 60 TNPPPSPLSL PAYPPSPSPL SPSIPPTYPP NTSPSPTTYP SSTSPTPSAN PPAYTSPSPS 120 PASSYAPSTS PIPIPPSHPP SASPPIYPSP SPSPSIPSPS YPTPSPSPSP SSSISSPPNY 180 PPSPSPSSSI SSPPRYPPSP SPSTAPSGLS VGYYRYSCPD AESIVRAAVK NATDGNRGTG 240 AGLIRLFFHD CFVEGCDASV LLNTTGSTRP TERASVPNLS LRGFEVIDAA KAALEAACPG 300 VVSCADIVAF AGRDATFFLS GNAVDFDMPA GRYDGHVSLD SAAIANLPPP FASLKELKDM 360 FAAKGLDTED MVTLSGAHTV GRSQCSSFSD RLPPNASDMN ATLAASLTSQ CNGTGDPTVP 420 QDFVTPSGLD SQYYRNVLNH EVLFGSDAAL LASDQTAGMV RDNAFKPGLW EDKFKAAMVK 480 MGRAGVKNST DGEIRKKCWM INQVSS* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00692 | ligninase | 2.0e-6 | 244 | 490 | 284 | + Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II 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 II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites. | ||
cd00314 | plant_peroxidase_like | 4.0e-20 | 223 | 483 | 291 | + 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-55 | 225 | 380 | 157 | + Peroxidase. | ||
PLN03030 | PLN03030 | 1.0e-69 | 208 | 502 | 308 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 3.0e-140 | 208 | 498 | 299 | + 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 |
DDBJ | BAF22325.2 | 0 | 138 | 504 | 55 | 419 | Os07g0638800 [Oryza sativa Japonica Group] |
GenBank | EAZ04858.1 | 0 | 197 | 502 | 76 | 384 | hypothetical protein OsI_27037 [Oryza sativa Indica Group] |
RefSeq | NP_001060411.1 | 0 | 208 | 502 | 90 | 384 | Os07g0638800 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002463261.1 | 0 | 211 | 502 | 326 | 618 | hypothetical protein SORBIDRAFT_02g040730 [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 | 3hdl_A | 0 | 209 | 502 | 2 | 303 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 1sch_B | 0 | 209 | 502 | 2 | 294 | A Chain A, Peanut Peroxidase |
PDB | 1sch_A | 0 | 209 | 502 | 2 | 294 | A Chain A, Peanut Peroxidase |
PDB | 1qo4_A | 0 | 209 | 502 | 3 | 304 | A Chain A, Peanut Peroxidase |
PDB | 1pa2_A | 0 | 209 | 502 | 3 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |