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Protein

Peroxidase

Gene
N/A
Organism
Arthromyces ramosus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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
Sitei72 – 721Transition state stabilizer
Active sitei76 – 761Proton acceptor
Metal bindingi77 – 771Calcium 1
Metal bindingi95 – 951Calcium 1; via carbonyl oxygen
Metal bindingi97 – 971Calcium 1
Metal bindingi99 – 991Calcium 1
Metal bindingi204 – 2041Iron (heme axial ligand)
Metal bindingi205 – 2051Calcium 2
Metal bindingi222 – 2221Calcium 2
Metal bindingi224 – 2241Calcium 2
Metal bindingi227 – 2271Calcium 2; via carbonyl oxygen
Metal bindingi229 – 2291Calcium 2

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

Enzyme and pathway databases

BRENDAi1.11.1.7. 462.

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiPRX2A_AGASP.
PeroxiBasei2404. ArCIIBA.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase (EC:1.11.1.7)
OrganismiArthromyces ramosus
Taxonomic identifieri5451 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricales

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 364344PeroxidasePRO_0000023666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid
Disulfide bondi32 ↔ 44
Disulfide bondi43 ↔ 313
Disulfide bondi63 ↔ 149
Glycosylationi163 – 1631N-linked (GlcNAc...) (high mannose)1 Publication
Disulfide bondi277 ↔ 342

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 393Combined sources
Helixi41 – 433Combined sources
Helixi44 – 5512Combined sources
Turni56 – 616Combined sources
Helixi65 – 7814Combined sources
Helixi83 – 875Combined sources
Beta strandi95 – 984Combined sources
Helixi99 – 1024Combined sources
Helixi104 – 1074Combined sources
Helixi111 – 1133Combined sources
Helixi117 – 13014Combined sources
Helixi134 – 14714Combined sources
Helixi180 – 19011Combined sources
Helixi194 – 2007Combined sources
Helixi201 – 2055Combined sources
Beta strandi208 – 2125Combined sources
Helixi214 – 2163Combined sources
Beta strandi219 – 2235Combined sources
Helixi231 – 2366Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi255 – 2573Combined sources
Helixi264 – 2718Combined sources
Turni273 – 2753Combined sources
Helixi276 – 2816Combined sources
Turni282 – 2843Combined sources
Helixi286 – 30015Combined sources
Turni301 – 3044Combined sources
Helixi307 – 3093Combined sources
Beta strandi310 – 3123Combined sources
Helixi314 – 3163Combined sources
Helixi330 – 3323Combined sources
Helixi335 – 3373Combined sources
Beta strandi343 – 3453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ARPX-ray1.90A21-364[»]
1ARUX-ray1.60A21-364[»]
1ARVX-ray1.60A21-364[»]
1ARWX-ray1.60A21-364[»]
1ARXX-ray1.90A21-364[»]
1ARYX-ray1.90A21-364[»]
1C8IX-ray2.00A21-364[»]
1CK6X-ray1.90A21-364[»]
1GZAX-ray2.06A21-364[»]
1GZBX-ray1.80A21-364[»]
1HSRX-ray1.60A21-364[»]
2E39X-ray1.30A21-364[»]
2E3AX-ray1.30A21-364[»]
2E3BX-ray1.30A21-364[»]
ProteinModelPortaliP28313.
SMRiP28313. Positions 29-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28313.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
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.

P28313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSLFSTFA AVIIGALALP QGPGGGGGSV TCPGGQSTSN SQCCVWFDVL
60 70 80 90 100
DDLQTNFYQG SKCESPVRKI LRIVFHDAIG FSPALTAAGQ FGGGGADGSI
110 120 130 140 150
IAHSNIELAF PANGGLTDTI EALRAVGINH GVSFGDLIQF ATAVGMSNCP
160 170 180 190 200
GSPRLEFLTG RSNSSQPSPP SLIPGPGNTV TAILDRMGDA GFSPDEVVDL
210 220 230 240 250
LAAHSLASQE GLNSAIFRSP LDSTPQVFDT QFYIETLLKG TTQPGPSLGF
260 270 280 290 300
AEELSPFPGE FRMRSDALLA RDSRTACRWQ SMTSSNEVMG QRYRAAMAKM
310 320 330 340 350
SVLGFDRNAL TDCSDVIPSA VSNNAAPVIP GGLTVDDIEV SCPSEPFPEI
360
ATASGPLPSL APAP
Length:364
Mass (Da):37,746
Last modified:October 1, 1996 - v3
Checksum:i08C3BB42B9695D88
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63792 mRNA. Translation: BAA09861.1.
PIRiS22221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63792 mRNA. Translation: BAA09861.1.
PIRiS22221.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ARPX-ray1.90A21-364[»]
1ARUX-ray1.60A21-364[»]
1ARVX-ray1.60A21-364[»]
1ARWX-ray1.60A21-364[»]
1ARXX-ray1.90A21-364[»]
1ARYX-ray1.90A21-364[»]
1C8IX-ray2.00A21-364[»]
1CK6X-ray1.90A21-364[»]
1GZAX-ray2.06A21-364[»]
1GZBX-ray1.80A21-364[»]
1HSRX-ray1.60A21-364[»]
2E39X-ray1.30A21-364[»]
2E3AX-ray1.30A21-364[»]
2E3BX-ray1.30A21-364[»]
ProteinModelPortaliP28313.
SMRiP28313. Positions 29-364.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiPRX2A_AGASP.
PeroxiBasei2404. ArCIIBA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.11.1.7. 462.

Miscellaneous databases

EvolutionaryTraceiP28313.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
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 nameiPER_ARTRA
AccessioniPrimary (citable) accession number: P28313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.