Skip Header

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

Peroxidase

Gene

CIP1

Organism
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
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
Sitei71 – 711Transition state stabilizer
Active sitei75 – 751Proton acceptor
Metal bindingi76 – 761Calcium 1
Metal bindingi94 – 941Calcium 1; via carbonyl oxygen
Metal bindingi96 – 961Calcium 1
Metal bindingi98 – 981Calcium 1
Metal bindingi203 – 2031Iron (heme axial ligand)
Metal bindingi204 – 2041Calcium 2
Metal bindingi221 – 2211Calcium 2
Metal bindingi223 – 2231Calcium 2
Metal bindingi226 – 2261Calcium 2; via carbonyl oxygen
Metal bindingi228 – 2281Calcium 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

Protein family/group databases

mycoCLAPiPRX2A_COPCI.
PeroxiBasei2403. CcinCIIBA.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase (EC:1.11.1.7)
Gene namesi
Name:CIP1
OrganismiCoprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Taxonomic identifieri5346 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

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 – 363343PeroxidasePRO_0000023667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid
Disulfide bondi31 ↔ 43
Disulfide bondi42 ↔ 312
Disulfide bondi62 ↔ 148
Glycosylationi162 – 1621N-linked (GlcNAc...) (high mannose)1 Publication
Disulfide bondi276 ↔ 341
Glycosylationi358 – 3581O-linked (Man...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 394Combined sources
Helixi40 – 423Combined sources
Helixi45 – 5410Combined sources
Turni55 – 606Combined sources
Helixi64 – 7714Combined sources
Helixi82 – 865Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 1014Combined sources
Helixi103 – 1064Combined sources
Helixi110 – 1123Combined sources
Helixi116 – 12914Combined sources
Helixi133 – 14614Combined sources
Helixi179 – 18911Combined sources
Helixi193 – 1997Combined sources
Helixi200 – 2056Combined sources
Beta strandi207 – 2115Combined sources
Helixi213 – 2153Combined sources
Beta strandi218 – 2225Combined sources
Helixi230 – 2356Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi254 – 2563Combined sources
Helixi263 – 2708Combined sources
Turni272 – 2743Combined sources
Helixi275 – 2806Combined sources
Helixi285 – 30016Combined sources
Turni301 – 3033Combined sources
Helixi306 – 3083Combined sources
Beta strandi309 – 3113Combined sources
Helixi313 – 3153Combined sources
Helixi334 – 3363Combined sources
Beta strandi342 – 3443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3JX-ray2.00A/B22-363[»]
1LY8X-ray2.05A/B21-363[»]
1LY9X-ray2.00A/B21-363[»]
1LYCX-ray1.57A/B21-363[»]
1LYKX-ray2.00A/B21-363[»]
ProteinModelPortaliP28314.
SMRiP28314. Positions 28-363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28314.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

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.

P28314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSLLSTFA AVIIGALALP QGPGGGGSVT CPGGQSTSNS QCCVWFDVLD
60 70 80 90 100
DLQTNFYQGS KCESPVRKIL RIVFHDAIGF SPALTAAGQF GGGGADGSII
110 120 130 140 150
AHSNIELAFP ANGGLTDTVE ALRAVGINHG VSFGDLIQFA TAVGMSNCPG
160 170 180 190 200
SPRLEFLTGR SNSSQPSPPS LIPGPGNTVT AILDRMGDAG FSPDEVVDLL
210 220 230 240 250
AAHSLASQEG LNSAIFRSPL DSTPQVFDTQ FYIETLLKGT TQPGPSLGFA
260 270 280 290 300
EELSPFPGEF RMRSDALLAR DSRTACRWQS MTSSNEVMGQ RYRAAMAKMS
310 320 330 340 350
VLGFDRNALT DCSDVIPSAV SNNAAPVIPG GLTVDDIEVS CPSEPFPEIA
360
TASGPLPSLA PAP
Length:363
Mass (Da):37,640
Last modified:July 1, 1993 - v2
Checksum:iE56EB53B963C3DB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191V → I in CAA50060 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991I → V.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69457 mRNA. Translation: CAA49216.1.
X70789 Genomic DNA. Translation: CAA50060.1.
PIRiS31780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69457 mRNA. Translation: CAA49216.1.
X70789 Genomic DNA. Translation: CAA50060.1.
PIRiS31780.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3JX-ray2.00A/B22-363[»]
1LY8X-ray2.05A/B21-363[»]
1LY9X-ray2.00A/B21-363[»]
1LYCX-ray1.57A/B21-363[»]
1LYKX-ray2.00A/B21-363[»]
ProteinModelPortaliP28314.
SMRiP28314. Positions 28-363.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiPRX2A_COPCI.
PeroxiBasei2403. CcinCIIBA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Miscellaneous databases

EvolutionaryTraceiP28314.

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...

Publicationsi

  1. "Amino acid sequence of Coprinus macrorhizus peroxidase and cDNA sequence encoding Coprinus cinereus peroxidase. A new family of fungal peroxidases."
    Baunsgaard L., Dalboege H., Houen G., Rasmussen E.M., Welinder K.G.
    Eur. J. Biochem. 213:605-611(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: NBRC 8371.
  2. Dalboege H.
    Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NBRC 8371.
  3. "Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus."
    Kjalke M., Andersen M.B., Schneider P., Christensen B., Schuelein M., Welinder K.G.
    Biochim. Biophys. Acta 1120:248-256(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 161-185.
  4. "Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6-A resolution."
    Petersen J.F.W., Kadziola A., Larsen S.
    FEBS Lett. 339:291-296(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), GLYCOSYLATION AT ASN-162 AND SER-358.
  5. "Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase."
    Houborg K., Harris P., Petersen J., Rowland P., Poulsen J.-C.N., Schneider P., Vind J., Larsen S.
    Acta Crystallogr. D 59:989-996(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS).
  6. "The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability."
    Houborg K., Harris P., Poulsen J.-C.N., Schneider P., Svendsen A., Larsen S.
    Acta Crystallogr. D 59:997-1003(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT.
  7. "The Asp245-->Asn mutant of Coprinus cinereus peroxidase. Characterization by 1H-NMR spectroscopy and comparison with the wild-type enzyme."
    Veitch N.C., Gao Y., Welinder K.G.
    Biochemistry 35:14370-14380(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF MUTANT ASN-265.

Entry informationi

Entry nameiPER_COPCI
AccessioniPrimary (citable) accession number: P28314
Secondary accession number(s): P28315, Q12575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 1, 1993
Last modified: November 11, 2015
This is version 110 of the entry and version 2 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.