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Protein

Peroxidase

Gene

CEVI-1

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.UniRule annotation
Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.SAAS annotation

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Ca2+UniRule annotationNote: Binds 2 calcium ions per subunit.UniRule annotation
  • heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxideUniRule annotation

Keywords - Ligandi

CalciumUniRule annotation, HemeUniRule annotationSAAS annotation, Iron, Metal-binding

Protein family/group databases

PeroxiBasei276. LePrx05.

Names & Taxonomyi

Protein namesi
Recommended name:
PeroxidaseUniRule annotationSAAS annotation (EC:1.11.1.7UniRule annotationSAAS annotation)
Gene namesi
Name:CEVI-1Imported
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)Imported
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Subcellular locationi

  • Secreted UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

SecretedUniRule annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222UniRule annotationAdd
BLAST
Chaini23 – 325303PeroxidaseUniRule annotationPRO_5005143287Add
BLAST

Keywords - PTMi

Disulfide bondSAAS annotation

Proteomic databases

PaxDbiQ43774.

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc01g006300.2.1.

Structurei

3D structure databases

ProteinModelPortaliQ43774.
SMRiQ43774. Positions 23-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 325303PEROXIDASE_4InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.UniRule annotationSAAS annotation

Keywords - Domaini

SignalUniRule annotation

Phylogenomic databases

eggNOGiENOG410J9DS. Eukaryota.
ENOG4111S7R. LUCA.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q43774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFLRFIFPL FFLISIFVAS NAQLSATFYA STCPNVTEIV RGVMQQAQST
60 70 80 90 100
VVRAGAKIIR LHFHDCFVNG CDGSLLLDNA AGIESEKDAA SNVGAGGFDI
110 120 130 140 150
VDDIKTALEN VCPGVVSCAD ILALASEIGV ALVGGPTWQV LLGRRDSLTA
160 170 180 190 200
NRSGVDSDIP TPFESLDVMR PQFTNKGMDI TDLVALSGAH TFGRARCGTF
210 220 230 240 250
QQRLFNFSGS GSPDPTINST YLPTLQATCP QGGNNGNTFE NLDKTTPDNF
260 270 280 290 300
DNDYYINLQN QEGLLQTDQE LFSTSGSDTI AIVNRYASSQ SQFFDDFASS
310 320
MIKLGNIGVL TGTNGEIRTD CKRVN
Length:325
Mass (Da):34,924
Last modified:November 1, 1996 - v1
Checksum:iCCF1A655355AC213
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71593 mRNA. Translation: CAA50597.1.
PIRiS32768.
UniGeneiLes.3608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71593 mRNA. Translation: CAA50597.1.
PIRiS32768.
UniGeneiLes.3608.

3D structure databases

ProteinModelPortaliQ43774.
SMRiQ43774. Positions 23-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc01g006300.2.1.

Protein family/group databases

PeroxiBasei276. LePrx05.

Proteomic databases

PaxDbiQ43774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410J9DS. Eukaryota.
ENOG4111S7R. LUCA.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression analysis of a viroid-induced peroxidase from tomato plants."
    Vera P., Torenero P., Conejero V.
    Mol. Plant Microbe Interact. 6:790-794(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: LeafImported.

Entry informationi

Entry nameiQ43774_SOLLC
AccessioniPrimary (citable) accession number: Q43774
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.