Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anionic peroxidase

Gene
N/A
Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. These functions might be dependent on each isozyme/isoform in each plant tissue.
May contribute to protection against cold-induced oxidative stress.

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei95 – 951Transition state stabilizerPROSITE-ProRule annotation
Active sitei99 – 991Proton acceptorPROSITE-ProRule annotation
Metal bindingi100 – 1001Calcium 1PROSITE-ProRule annotation
Metal bindingi103 – 1031Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi105 – 1051Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi107 – 1071Calcium 1PROSITE-ProRule annotation
Metal bindingi227 – 2271Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi228 – 2281Calcium 2PROSITE-ProRule annotation
Metal bindingi268 – 2681Calcium 2PROSITE-ProRule annotation
Metal bindingi270 – 2701Calcium 2PROSITE-ProRule annotation
Metal bindingi275 – 2751Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei66. IbPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Anionic peroxidase (EC:1.11.1.7)
Alternative name(s):
SwPA1
OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifieri4120 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 66461 PublicationPRO_0000023749Add
BLAST
Chaini67 – 364298Anionic peroxidasePRO_0000023750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi101 ↔ 106PROSITE-ProRule annotation
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi155 ↔ 343PROSITE-ProRule annotation
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence analysis
Disulfide bondi234 ↔ 255PROSITE-ProRule annotation
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Highly expressed in suspension cultured cells and calli. Weak expression also found in the stems of intact plants. No expression in leaf, tuberous root and non-tuberous root.

Developmental stagei

Highly expressed 0.5 days after subculture (DAS). No expression was detected at 5 DAS and then expression was highly induced between 11-20 DAS.

Inductioni

By wounding and cold stress. Weakly induced by acclimation and strongly induced by chilling treatment.

Structurei

3D structure databases

ProteinModelPortaliO04795.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFMKQLSL VLSFIALALA GCAVYQNTQT AMKDQLKVTP TWLDNTLKST
60 70 80 90 100
NLLSLGLGKP SGGKLGDEAC VFSAVKEVVV AAINAEARMG ASLIRLFFHD
110 120 130 140 150
CFVDGCDAGL LLNDTATFTG EQTAAGNNNS VRGFAVIEQA KQNVKTQMPD
160 170 180 190 200
MSVSCADILS IAARDSFEKF SGSTYTVTLG RKDARTANFT GANTQLVGPN
210 220 230 240 250
ENLTSQLTKF AAKGFNGTEM VALLGSHTIG FARCPLLCIS TFINPARVST
260 270 280 290 300
LNCNCSGTVN ATGLVGLDPT PTTWDQRYFS DVVNDQGLLF SDNELLKGNT
310 320 330 340 350
TNAAVRRYRD AMGAFLTDFA AAMVKMSNLP PSPGVALEIR DVCSRVNANS
360
VDPCEESRLL ASPD
Length:364
Mass (Da):38,693
Last modified:July 1, 1997 - v1
Checksum:i5D1DC936E3F1F8D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z84472 mRNA. Translation: CAB06477.1.
PIRiT10945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z84472 mRNA. Translation: CAB06477.1.
PIRiT10945.

3D structure databases

ProteinModelPortaliO04795.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei66. IbPrx01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Entry informationi

Entry nameiPERA_IPOBA
AccessioniPrimary (citable) accession number: O04795
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Lacks one of the disulfide bridges highly conserved in the class III peroxidase family.Curated

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.