Peroxidase 2 - Cucumis sativus (Cucumber)

Contribute

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P19135 (PER2_CUCSA)

Last modified June 16, 2009. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Peroxidase 2 EC=1.11.1.7 Alternative name(s): CUP2
Organism	Cucumis sativus (Cucumber)
Taxonomic identifier	3659 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Cucumis

Protein attributes

Sequence length	292 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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.
Catalytic activity	Donor + H₂O₂ = oxidized donor + 2 H₂O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

›292

Peroxidase 2

PRO_0000055610

Sites

Active site

1

Proton acceptor By similarity

Metal binding

1

Calcium 1 By similarity

Metal binding

1

Calcium 1; via carbonyl oxygen By similarity

Metal binding

1

Calcium 1; via carbonyl oxygen By similarity

Metal binding

1

Calcium 1 By similarity

Metal binding

1

Calcium 1 By similarity

Metal binding

1

Iron (heme axial ligand) By similarity

Metal binding

1

Calcium 2 By similarity

Metal binding

1

Calcium 2 By similarity

Metal binding

1

Calcium 2 By similarity

Metal binding

1

Calcium 2 By similarity

Binding site

1

Substrate; via carbonyl oxygen By similarity

Site

1

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Experimental info

Non-terminal residue

1

Sequences

Sequence

Length

Mass (Da)

Tools

P19135-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 98FD89EF01CE6888
Show »

292

31,857

        10         20         30         40         50         60 
TFYDESCPDV SNIVRRVVQQ ALVSDERAGA RLIRLHFHDC FVNGCDGSVL LEDQPGVVSE 

        70         80         90        100        110        120 
LAAPGNANIT GFNIVNNIKA AVEKACPGVV SCADILAIAS VGSVNLAGGP CWEVQLGRRD 

       130        140        150        160        170        180 
SRRANLQGAI DGLPSPFENV TQLKRKFDRV DLDSTDLVAL SGAHTFGKSR CQFFDRRLNV 

       190        200        210        220        230        240 
SNPDSTLNPR YAQQLRQACS SGRDTFVNLD PTTPNKFDKN YYTNLQSNTG PLTSDQVLHS 

       250        260        270        280        290 
TPGEDTVKIV NLFAASQNQF FESFGQSMIN MGNIQPLTGN QGEIRSNCRR LN

References

[1]	"Isolation and sequencing of cDNA clones encoding ethylene-induced putative peroxidases from cucumber cotyledons." Morgens P.H., Callahan A.M., Dunn L.J., Abeles F.B. Plant Mol. Biol. 14:715-725(1990) [PubMed: 2102850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
	M32742 mRNA. Translation: AAA33121.1.
PIR	S11870.
3D structure databases
HSSP	HSSP built from PDB template 1PA2 based on UniProtKB Q42578.
ModBase	Search...
Protein family/group databases
PeroxiBase	23. CsaPrx07.
Enzyme and pathway databases
BRENDA	1.11.1.7. 1241.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER2_CUCSA

Accession

Primary (citable) accession number: P19135

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents