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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)DescriptionActionsGraphical viewLength
Sitei72Transition state stabilizer1
Active sitei76Proton acceptor1
Metal bindingi77Calcium 11
Metal bindingi95Calcium 1; via carbonyl oxygen1
Metal bindingi97Calcium 11
Metal bindingi99Calcium 11
Metal bindingi204Iron (heme axial ligand)1
Metal bindingi205Calcium 21
Metal bindingi222Calcium 21
Metal bindingi224Calcium 21
Metal bindingi227Calcium 2; via carbonyl oxygen1
Metal bindingi229Calcium 21

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000002366621 – 364PeroxidaseAdd BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acid1
Disulfide bondi32 ↔ 44
Disulfide bondi43 ↔ 313
Disulfide bondi63 ↔ 149
Glycosylationi163N-linked (GlcNAc...) (high mannose)1 Publication1
Disulfide bondi277 ↔ 342

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 39Combined sources3
Helixi41 – 43Combined sources3
Helixi44 – 55Combined sources12
Turni56 – 61Combined sources6
Helixi65 – 78Combined sources14
Helixi83 – 87Combined sources5
Beta strandi95 – 98Combined sources4
Helixi99 – 102Combined sources4
Helixi104 – 107Combined sources4
Helixi111 – 113Combined sources3
Helixi117 – 130Combined sources14
Helixi134 – 147Combined sources14
Helixi180 – 190Combined sources11
Helixi194 – 200Combined sources7
Helixi201 – 205Combined sources5
Beta strandi208 – 212Combined sources5
Helixi214 – 216Combined sources3
Beta strandi219 – 223Combined sources5
Helixi231 – 236Combined sources6
Beta strandi245 – 247Combined sources3
Beta strandi255 – 257Combined sources3
Helixi264 – 271Combined sources8
Turni273 – 275Combined sources3
Helixi276 – 281Combined sources6
Turni282 – 284Combined sources3
Helixi286 – 300Combined sources15
Turni301 – 304Combined sources4
Helixi307 – 309Combined sources3
Beta strandi310 – 312Combined sources3
Helixi314 – 316Combined sources3
Helixi330 – 332Combined sources3
Helixi335 – 337Combined sources3
Beta strandi343 – 345Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28313.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 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
PDB 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.
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

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 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: November 30, 2016
This is version 114 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.