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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi56 – 561Manganese
Metal bindingi60 – 601Manganese
Sitei63 – 631Transition state stabilizer
Active sitei67 – 671Proton acceptor
Metal bindingi68 – 681Calcium 1
Metal bindingi83 – 831Calcium 1; via carbonyl oxygen
Metal bindingi85 – 851Calcium 1
Metal bindingi87 – 871Calcium 1
Metal bindingi194 – 1941Iron (heme axial ligand)
Metal bindingi195 – 1951Calcium 2
Metal bindingi200 – 2001Manganese
Metal bindingi212 – 2121Calcium 2
Metal bindingi214 – 2141Calcium 2
Metal bindingi217 – 2171Calcium 2; via carbonyl oxygen
Metal bindingi219 – 2191Calcium 2

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

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 378357Manganese peroxidase 1PRO_0000023778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 36
Disulfide bondi35 ↔ 310
Disulfide bondi54 ↔ 138
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)
Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence analysis
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

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 273Combined sources
Helixi33 – 375Combined sources
Helixi38 – 4811Combined sources
Turni49 – 524Combined sources
Beta strandi53 – 553Combined sources
Helixi56 – 7015Combined sources
Turni74 – 763Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 853Combined sources
Helixi87 – 904Combined sources
Turni92 – 943Combined sources
Helixi95 – 973Combined sources
Helixi99 – 1013Combined sources
Turni102 – 1043Combined sources
Helixi105 – 11713Combined sources
Helixi123 – 13614Combined sources
Helixi169 – 18012Combined sources
Helixi184 – 1907Combined sources
Helixi191 – 1966Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi209 – 2135Combined sources
Helixi221 – 2266Combined sources
Helixi261 – 2688Combined sources
Turni270 – 2723Combined sources
Helixi273 – 2786Combined sources
Turni279 – 2813Combined sources
Helixi283 – 29715Combined sources
Turni298 – 3014Combined sources
Helixi304 – 3063Combined sources
Beta strandi307 – 3093Combined sources
Helixi311 – 3133Combined sources
Helixi333 – 3353Combined sources
Beta strandi365 – 3673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 22-378.
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.
OMAiHANDGID.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751S → L in AAA33742 (PubMed:2925681).Curated

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
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. Positions 22-378.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiMPO2A_PHACH.
PeroxiBasei3866. PcMnP01_OGC101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZ9A. Eukaryota.
ENOG410YEPY. LUCA.
OMAiHANDGID.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ02567.

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. "Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium."
    Godfrey B.J., Mayfield M.B., Brown J.A., Gold M.H.
    Gene 93:119-124(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 201542 / OGC101.
  2. "Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium."
    Pribnow D., Mayfield M.B., Nipper V.J., Brown J.A., Gold M.H.
    J. Biol. Chem. 264:5036-5040(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-41.
    Strain: ATCC 201542 / OGC101.
  3. "Characterization of manganese(II) binding site mutants of manganese peroxidase."
    Kishi K., Kusters-van Someren M., Mayfield M.B., Sun J., Loehr T.M., Gold M.H.
    Biochemistry 35:8986-8994(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: METAL-BINDING.
  4. "The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution."
    Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.
    J. Biol. Chem. 269:32759-32767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
  5. "Crystal structures of substrate binding site mutants of manganese peroxidase."
    Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.
    J. Biol. Chem. 272:17574-17580(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.

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: December 9, 2015
This is version 117 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.