SubmitCancel

Skip Header

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

P48534

- APX1_PEA

UniProt

P48534 - APX1_PEA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
L-ascorbate peroxidase, cytosolic
Gene
APX1, APPX1
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a key role in hydrogen peroxide removal.

Catalytic activityi

2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O.

Cofactori

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei38 – 381Transition state stabilizer
Active sitei42 – 421Proton acceptor
Metal bindingi163 – 1631Iron (heme axial ligand)1 Publication
Metal bindingi164 – 1641Potassium or calcium
Metal bindingi180 – 1801Potassium or calcium
Metal bindingi182 – 1821Potassium or calcium
Metal bindingi185 – 1851Potassium or calcium; via carbonyl oxygen
Metal bindingi187 – 1871Potassium or calcium

GO - Molecular functioni

  1. L-ascorbate peroxidase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Stress response

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding, Potassium

Enzyme and pathway databases

SABIO-RKP48534.

Protein family/group databases

PeroxiBasei2462. PsAPx01.

Names & Taxonomyi

Protein namesi
Recommended name:
L-ascorbate peroxidase, cytosolic (EC:1.11.1.11)
Short name:
AP
Alternative name(s):
PsAPx01
Gene namesi
Name:APX1
Synonyms:APPX1
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 250249L-ascorbate peroxidase, cytosolic
PRO_0000055597Add
BLAST

Proteomic databases

ProMEXiP48534.

Expressioni

Inductioni

By stress.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3021
Helixi33 – 4412
Turni49 – 524
Beta strandi55 – 584
Helixi59 – 613
Helixi63 – 664
Helixi69 – 713
Helixi74 – 8613
Helixi93 – 10715
Helixi138 – 1458
Turni146 – 1483
Helixi153 – 1608
Helixi161 – 1644
Turni170 – 1723
Beta strandi177 – 1815
Helixi189 – 1957
Helixi206 – 2094
Turni210 – 2123
Helixi217 – 22610
Helixi228 – 24316
Turni244 – 2463

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APXX-ray2.20A/B/C/D2-250[»]
ProteinModelPortaliP48534.
SMRiP48534. Positions 2-250.

Miscellaneous databases

EvolutionaryTraceiP48534.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
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.

P48534-1 [UniParc]FASTAAdd to Basket

« Hide

MGKSYPTVSP DYQKAIEKAK RKLRGFIAEK KCAPLILRLA WHSAGTFDSK    50
TKTGGPFGTI KHQAELAHGA NNGLDIAVRL LEPIKEQFPI VSYADFYQLA 100
GVVAVEITGG PEVPFHPGRE DKPEPPPEGR LPDATKGSDH LRDVFGKAMG 150
LSDQDIVALS GGHTIGAAHK ERSGFEGPWT SNPLIFDNSY FTELLTGEKD 200
GLLQLPSDKA LLTDSVFRPL VEKYAADEDV FFADYAEAHL KLSELGFAEA 250
Length:250
Mass (Da):27,193
Last modified:January 23, 2007 - v2
Checksum:i6F51006D0A13B42C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93051 Genomic DNA. Translation: AAA33645.1.
X62077 mRNA. Translation: CAA43992.1.
PIRiA45116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93051 Genomic DNA. Translation: AAA33645.1 .
X62077 mRNA. Translation: CAA43992.1 .
PIRi A45116.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APX X-ray 2.20 A/B/C/D 2-250 [» ]
ProteinModelPortali P48534.
SMRi P48534. Positions 2-250.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PeroxiBasei 2462. PsAPx01.

Proteomic databases

ProMEXi P48534.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P48534.

Miscellaneous databases

EvolutionaryTracei P48534.

Family and domain databases

InterProi IPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view ]
Pfami PF00141. peroxidase. 1 hit.
[Graphical view ]
PRINTSi PR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase."
    Mittler R., Zilinskas B.A.
    FEBS Lett. 289:257-259(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Little Marvel.
    Tissue: Leaf.
  2. "Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase."
    Mittler R., Zilinskas B.A.
    J. Biol. Chem. 267:21802-21807(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: cv. Little Marvel.
  3. Erratum
    Mittler R., Zilinskas B.A.
    J. Biol. Chem. 268:4568-4568(1993)
  4. "Crystal structure of recombinant pea cytosolic ascorbate peroxidase."
    Patterson W.R., Poulos T.L.
    Biochemistry 34:4331-4341(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEME AND POTASSIUM IONS.

Entry informationi

Entry nameiAPX1_PEA
AccessioniPrimary (citable) accession number: P48534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds one cation per subunit; probably K+, but might also be Ca2+.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi