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Protein

L-ascorbate peroxidase, cytosolic

Gene

APX1

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: 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

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei38Transition state stabilizer1
Active sitei42Proton acceptor1
Metal bindingi163Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication1
Metal bindingi164Potassium or calcium1
Metal bindingi180Potassium or calcium1
Metal bindingi182Potassium or calcium1
Metal bindingi185Potassium or calcium; via carbonyl oxygen1
Metal bindingi187Potassium or calcium1

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000555972 – 250L-ascorbate peroxidase, cytosolicAdd BLAST249

Proteomic databases

PRIDEiP48534.

Expressioni

Inductioni

By stress.1 Publication

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 30Combined sources21
Helixi33 – 44Combined sources12
Turni49 – 52Combined sources4
Beta strandi55 – 58Combined sources4
Helixi59 – 61Combined sources3
Helixi63 – 66Combined sources4
Helixi69 – 71Combined sources3
Helixi74 – 86Combined sources13
Helixi93 – 107Combined sources15
Helixi138 – 145Combined sources8
Turni146 – 148Combined sources3
Helixi153 – 160Combined sources8
Helixi161 – 164Combined sources4
Turni170 – 172Combined sources3
Beta strandi177 – 181Combined sources5
Helixi189 – 195Combined sources7
Helixi206 – 209Combined sources4
Turni210 – 212Combined sources3
Helixi217 – 226Combined sources10
Helixi228 – 243Combined sources16
Turni244 – 246Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APXX-ray2.20A/B/C/D2-250[»]
ProteinModelPortaliP48534.
SMRiP48534.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MGKSYPTVSP DYQKAIEKAK RKLRGFIAEK KCAPLILRLA WHSAGTFDSK
60 70 80 90 100
TKTGGPFGTI KHQAELAHGA NNGLDIAVRL LEPIKEQFPI VSYADFYQLA
110 120 130 140 150
GVVAVEITGG PEVPFHPGRE DKPEPPPEGR LPDATKGSDH LRDVFGKAMG
160 170 180 190 200
LSDQDIVALS GGHTIGAAHK ERSGFEGPWT SNPLIFDNSY FTELLTGEKD
210 220 230 240 250
GLLQLPSDKA LLTDSVFRPL VEKYAADEDV FFADYAEAHL KLSELGFAEA
Length:250
Mass (Da):27,193
Last modified:January 23, 2007 - v2
Checksum:i6F51006D0A13B42C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93051 Genomic DNA. Translation: AAA33645.1.
X62077 mRNA. Translation: CAA43992.1.
PIRiA45116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93051 Genomic DNA. Translation: AAA33645.1.
X62077 mRNA. Translation: CAA43992.1.
PIRiA45116.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APXX-ray2.20A/B/C/D2-250[»]
ProteinModelPortaliP48534.
SMRiP48534.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei2462. PsAPx01.

Proteomic databases

PRIDEiP48534.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP48534.

Miscellaneous databases

EvolutionaryTraceiP48534.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 102 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

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.