Peroxidase manganese-dependent H3 precursor - Phanerochaete chrysosporium (White-rot fungus)

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Reviewed, UniProtKB/Swiss-Prot P78733 (PEM3_PHACH)

Last modified November 25, 2008. Version 52. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Peroxidase manganese-dependent H3 EC=1.11.1.13
Organism	Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier	5306 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.
Catalytic activity	2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peroxidase family. Ligninase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide Lignin degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Manganese Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

25

Chain

355

Peroxidase manganese-dependent H3

PRO_0000023779

Sites

Active site

1

Proton acceptor By similarity

Metal binding

1

Manganese By similarity

Metal binding

1

Manganese By similarity

Metal binding

1

Calcium 1 By similarity

Metal binding

1

Calcium 1; via carbonyl oxygen By similarity

Metal binding

1

Calcium 1 By similarity

Metal binding

1

Calcium 1 By similarity

Metal binding

1

Iron (heme axial ligand) By similarity

Metal binding

1

Calcium 2 By similarity

Metal binding

1

Manganese By similarity

Metal binding

1

Calcium 2 By similarity

Metal binding

1

Calcium 2 By similarity

Metal binding

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

1

Calcium 2 By similarity

Site

1

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P78733-1 [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: 4C8931EA3940BBA6
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380

40,078

        10         20         30         40         50         60 
MAFASSLLAL VALAAVTSAA PATTQATCPD GTKVNNAACC AFIPLAQDLQ ETIFQNDCGE 

        70         80         90        100        110        120 
DAHEVIRLTF HDAIAISQSK GPSAGGADGS MLLFPTIEPN FSANNGIDDS VNNLIPFMQK 

       130        140        150        160        170        180 
HNTISAGDIV QFTGAVALTN CPGAPQLEFL ARRPNKTIPA IDGLIPEPQD SVTSILERFK 

       190        200        210        220        230        240 
DAGNFSPFEV VSLLASHSVA RADKVDETID AAPFDTTPFV FDTQIFLEVL LKGVGFPGTR 

       250        260        270        280        290        300 
TTRGEVASPL PLTSGSDTGE LRLQSDFALA RDERTACIWQ GFVNEQALMA SFKAAMRKLA 

       310        320        330        340        350        360 
VLGQHRNTLI DCSDVVPAPK PAVNKPASFP ATTGPQDLEL SCNTKPFPSL SVDAGAQQTL 

       370        380 
IPHCSDGDMT CQSVQFNGPA

References

[1]	"Characterization of a cDNA encoding a manganese peroxidase from Phanerochaete chrysosporium: genomic organization of lignin and manganese peroxidase-encoding genes." Orth A.B., Rzhetskaya M., Cullen D., Tien M. Gene 148:161-165(1994) [PubMed: 7926830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
[2]	"Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium." Pease E.A., Tien M. J. Bacteriol. 174:3532-3540(1992) [PubMed: 1592808] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-45.

Cross-references

Sequence databases
	U10306 mRNA. Translation: AAA62243.1.
PIR	JC2579.
3D structure databases
HSSP	HSSP built from PDB template 1MN2 based on UniProtKB Q02567.
SMR	P78733. Positions 26-380.
ModBase	Search...
Protein family/group databases
PeroxiBase	2382. PcMnP04.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR001621. Ligninase. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00462. LIGNINASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEM3_PHACH

Accession

Primary (citable) accession number: P78733
Secondary accession number(s): Q01666

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	July 5, 2004
Last modified:	November 25, 2008
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents