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Protein

Manganese peroxidase 1

Gene

MNP1

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of Mn2+ to Mn3+. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.

Catalytic activityi

2 Mn2+ + 2 H+ + H2O2 = 2 Mn3+ + 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
Metal bindingi56Manganese1
Metal bindingi60Manganese1
Sitei63Transition state stabilizer1
Active sitei67Proton acceptor1
Metal bindingi68Calcium 11
Metal bindingi83Calcium 1; via carbonyl oxygen1
Metal bindingi85Calcium 11
Metal bindingi87Calcium 11
Metal bindingi194Iron (heme axial ligand)1
Metal bindingi195Calcium 21
Metal bindingi200Manganese1
Metal bindingi212Calcium 21
Metal bindingi214Calcium 21
Metal bindingi217Calcium 2; via carbonyl oxygen1
Metal bindingi219Calcium 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Lignin degradation

Keywords - Ligandi

Calcium, Heme, Iron, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14335.
BRENDAi1.11.1.13. 1380.
SABIO-RKQ02567.

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiMPO2A_PHACH.
PeroxiBasei3866. PcMnP01_OGC101.

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese peroxidase 1 (EC:1.11.1.13)
Short name:
MnP-1
Short name:
MnP1
Alternative name(s):
Manganese peroxidase isozyme 1
Peroxidase manganese-dependent 1
Peroxidase manganese-dependent I
Gene namesi
Name:MNP1
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000002377822 – 378Manganese peroxidase 1Add BLAST357

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 36
Disulfide bondi35 ↔ 310
Disulfide bondi54 ↔ 138
Glycosylationi97N-linked (GlcNAc...)Sequence analysis1
Glycosylationi152N-linked (GlcNAc...)1
Glycosylationi238N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi274 ↔ 340
Disulfide bondi362 ↔ 369

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

During wound-healing and by factors which induce suberization.

Structurei

Secondary structure

1378
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 27Combined sources3
Helixi33 – 37Combined sources5
Helixi38 – 48Combined sources11
Turni49 – 52Combined sources4
Beta strandi53 – 55Combined sources3
Helixi56 – 70Combined sources15
Turni74 – 76Combined sources3
Helixi78 – 80Combined sources3
Beta strandi83 – 85Combined sources3
Helixi87 – 90Combined sources4
Turni92 – 94Combined sources3
Helixi95 – 97Combined sources3
Helixi99 – 101Combined sources3
Turni102 – 104Combined sources3
Helixi105 – 117Combined sources13
Helixi123 – 136Combined sources14
Helixi169 – 180Combined sources12
Helixi184 – 190Combined sources7
Helixi191 – 196Combined sources6
Beta strandi198 – 203Combined sources6
Beta strandi209 – 213Combined sources5
Helixi221 – 226Combined sources6
Helixi261 – 268Combined sources8
Turni270 – 272Combined sources3
Helixi273 – 278Combined sources6
Turni279 – 281Combined sources3
Helixi283 – 297Combined sources15
Turni298 – 301Combined sources4
Helixi304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Helixi311 – 313Combined sources3
Helixi333 – 335Combined sources3
Beta strandi365 – 367Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MN1X-ray2.00A22-378[»]
1MN2X-ray2.00A22-378[»]
1MNPX-ray2.00A22-378[»]
1YYDX-ray1.45A22-378[»]
1YYGX-ray1.60A22-378[»]
1YZPX-ray1.60A22-378[»]
1YZRX-ray1.60A22-378[»]
3M5QX-ray0.93A22-378[»]
3M8MX-ray1.05A22-378[»]
ProteinModelPortaliQ02567.
SMRiQ02567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02567.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IZ9A. Eukaryota.
ENOG410YEPY. LUCA.
OMAiCITHAGR.

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.

Q02567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFKSLIAFV ALAAAVRAAP TAVCPDGTRV SHAACCAFIP LAQDLQETIF
60 70 80 90 100
QNECGEDAHE VIRLTFHDAI AISRSQGPKA GGGADGSMLL FPTVEPNFSA
110 120 130 140 150
NNGIDDSVNN LIPFMQKHNT ISAADLVQFA GAVALSNCPG APRLEFLAGR
160 170 180 190 200
PNKTIAAVDG LIPEPQDSVT KILQRFEDAG GFTPFEVVSL LASHSVARAD
210 220 230 240 250
KVDQTIDAAP FDSTPFTFDT QVFLEVLLKG VGFPGSANNT GEVASPLPLG
260 270 280 290 300
SGSDTGEMRL QSDFALAHDP RTACIWQGFV NEQAFMAASF RAAMSKLAVL
310 320 330 340 350
GHNRNSLIDC SDVVPVPKPA TGQPAMFPAS TGPQDLELSC PSERFPTLTT
360 370
QPGASQSLIA HCPDGSMSCP GVQFNGPA
Length:378
Mass (Da):39,557
Last modified:November 1, 1996 - v1
Checksum:i17A9A8F642441F27
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti75S → L in AAA33742 (PubMed:2925681).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60672 Genomic DNA. Translation: AAA33744.1.
M77513 Genomic DNA. Translation: AAA33743.1.
J04624 mRNA. Translation: AAA33742.1.
PIRiJN0092. A33271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60672 Genomic DNA. Translation: AAA33744.1.
M77513 Genomic DNA. Translation: AAA33743.1.
J04624 mRNA. Translation: AAA33742.1.
PIRiJN0092. A33271.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MN1X-ray2.00A22-378[»]
1MN2X-ray2.00A22-378[»]
1MNPX-ray2.00A22-378[»]
1YYDX-ray1.45A22-378[»]
1YYGX-ray1.60A22-378[»]
1YZPX-ray1.60A22-378[»]
1YZRX-ray1.60A22-378[»]
3M5QX-ray0.93A22-378[»]
3M8MX-ray1.05A22-378[»]
ProteinModelPortaliQ02567.
SMRiQ02567.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiMPO2A_PHACH.
PeroxiBasei3866. PcMnP01_OGC101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZ9A. Eukaryota.
ENOG410YEPY. LUCA.
OMAiCITHAGR.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14335.
BRENDAi1.11.1.13. 1380.
SABIO-RKQ02567.

Miscellaneous databases

EvolutionaryTraceiQ02567.

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 nameiPEM1_PHACH
AccessioniPrimary (citable) accession number: Q02567
Secondary accession number(s): Q01788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 121 of the entry and version 1 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.