[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 31-47, FUNCTION, AND SUBCELLULAR LOCATION. STRAIN=ATCC 90787 / IJFM A169 / CBS 613.91; PubMed=9987124 [NCBI, ExPASy, EBI, Israel, Japan] Ruiz-Duenas F.J., Martinez M.J., Martinez A.T.; "Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii."; Mol. Microbiol. 31:223-235(1999).
[2]	STRUCTURE BY NMR, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF ASP-205. STRAIN=ATCC 90787 / IJFM A169 / CBS 613.91; DOI=10.1007/s00775-003-0476-1; PubMed=12884090 [NCBI, ExPASy, EBI, Israel, Japan] Banci L., Camarero S., Martinez A.T., Martinez M.J., Perez-Boada M., Pierattelli R., Ruiz-Duenas F.J.; "NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii."; J. Biol. Inorg. Chem. 8:751-760(2003).
[3]	X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 31-361 OF WILD-TYPE AND MUTANT SER-194 IN COMPLEX WITH HEME; MANGANESE AND CALCIUM IONS, DISULFIDE BONDS, RADICAL INTERMEDIATE, CATALYTIC MECHANISM, AND MUTAGENESIS OF PRO-106; TRP-194 AND HIS-262. STRAIN=ATCC 90787 / IJFM A169 / CBS 613.91; DOI=10.1016/j.jmb.2005.09.047; PubMed=16246366 [NCBI, ExPASy, EBI, Israel, Japan] Perez-Boada M., Ruiz-Duenas F.J., Pogni R., Basosi R., Choinowski T., Martinez M.J., Piontek K., Martinez A.T.; "Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways."; J. Mol. Biol. 354:385-402(2005).

Comments

FUNCTION: A versatile ligninolytic peroxidase that combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.
CATALYTIC ACTIVITY: Reactive Black 5 + H₂O₂ = oxidized Reactive Black 5 + 2 H₂O.
CATALYTIC ACTIVITY: Donor + H₂O₂ = oxidized donor + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
COFACTOR: Binds 2 calcium ions per subunit.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=19 µM for manganese;
K_M=3000 µM for veratryl alcohol;
K_M=4 µM for reactive black 5;
K_M=3 µM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS);
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF007222; AAD01402.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF007224; AAD01404.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

2BOQ; X-ray; 1.33 A; A=31-361.	[ExPASy / RCSB / EBI]
2VKA; X-ray; 2.00 A; A=31-347.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2BOQ; -.
2VKA; -.

ModBase

O94753.

Protein family/group databases

PeroxiBase

2299; PerVP02.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0033747;	Molecular function: versatile peroxidase activity (inferred from electronic annotation from EC).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0046274;	Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002016; Haem_peroxidase_pln/fun/bac.
IPR001621; Ligninase.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00462; LIGNINASE.
PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

O94753.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; Manganese; Metal-binding; Organic radical; Oxidoreductase; Peroxidase; Secreted; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`PROPEP`	`23 30`	`8`		`PRO_0000308171`
`CHAIN`	`31 361`	`331`	`Versatile peroxidase VPL2.`	`PRO_5000053247`
`REGION`	`203 207`	`5`	`Heme binding.`
`ACT_SITE`	`77 77`		`Proton acceptor (By similarity).`
`ACT_SITE`	`194 194`		`Tryptophan radical intermediate.`
`METAL`	`66 66`		`Manganese.`
`METAL`	`70 70`		`Manganese (By similarity).`
`METAL`	`78 78`		`Calcium 1.`
`METAL`	`90 90`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`92 92`		`Calcium 1.`
`METAL`	`94 94`		`Calcium 1.`
`METAL`	`199 199`		`Iron (heme axial ligand).`
`METAL`	`200 200`		`Calcium 2.`
`METAL`	`205 205`		`Manganese.`
`METAL`	`217 217`		`Calcium 2.`
`METAL`	`219 219`		`Calcium 2.`
`METAL`	`222 222`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`224 224`		`Calcium 2.`
`SITE`	`73 73`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`126 126`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`33 45`
`DISULFID`	`44 308`
`DISULFID`	`64 144`
`DISULFID`	`272 337`
`MUTAGEN`	`106 106`		`P->H: Minor effects on activity.`
`MUTAGEN`	`194 194`		`W->H,S: Complete loss of activity toward veratryl alcohol and reactive black 5. No effect on manganese oxidation.`
`MUTAGEN`	`205 205`		`D->A: Complete loss of oxidation activity toward manganese.`
`MUTAGEN`	`262 262`		`H->F: Minor effects on activity.`
`HELIX`	`42 46`	`5`
`HELIX`	`47 57`	`11`
`TURN`	`60 62`	`3`
`HELIX`	`66 79`	`14`
`TURN`	`84 86`	`3`
`STRAND`	`90 93`	`4`
`HELIX`	`94 97`	`4`
`HELIX`	`99 102`	`4`
`HELIX`	`106 108`	`3`
`TURN`	`109 111`	`3`
`HELIX`	`112 124`	`13`
`STRAND`	`125 127`	`3`
`HELIX`	`129 142`	`14`
`HELIX`	`175 184`	`10`
`HELIX`	`189 195`	`7`
`HELIX`	`196 201`	`6`
`STRAND`	`203 208`	`6`
`STRAND`	`214 218`	`5`
`HELIX`	`226 230`	`5`
`STRAND`	`250 252`	`3`
`HELIX`	`259 264`	`6`
`TURN`	`268 270`	`3`
`HELIX`	`271 276`	`6`
`TURN`	`277 279`	`3`
`HELIX`	`281 296`	`16`
`TURN`	`297 299`	`3`
`HELIX`	`302 304`	`3`
`STRAND`	`305 307`	`3`
`HELIX`	`309 311`	`3`
`HELIX`	`330 332`	`3`
`STRAND`	`338 340`	`3`

Sequence information

Length: 361 AA [This is the length of the unprocessed precursor]

Molecular weight: 37624 Da [This is the MW of the unprocessed precursor]

CRC64: 18C4C6900F22A1E5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFKTLSALA LALGAAVQFA SAAVPLVQKR ATCDDGRTTA NAACCILFPI LDDIQENLFD 

        70         80         90        100        110        120 
GAQCGEEVHE SLRLTFHDAI GFSPTLGGGG ADGSIIAFDT IETNFPANAG IDEIVSAQKP 

       130        140        150        160        170        180 
FVAKHNISAG DFIQFAGAVG VSNCPGGVRI PFFLGRPDAV AASPDHLVPE PFDSVDSILA 

       190        200        210        220        230        240 
RMGDAGFSPV EVVWLLASHS IAAADKVDPS IPGTPFDSTP GVFDSQFFIE TQLKGRLFPG 

       250        260        270        280        290        300 
TADNKGEAQS PLQGEIRLQS DHLLARDPQT ACEWQSMVNN QPKIQNRFAA TMSKMALLGQ 

       310        320        330        340        350        360 
DKTKLIDCSD VIPTPPALVG AAHLPAGFSL SDVEQACAAT PFPALTADPG PVTSVPPVPG 


S

O94753 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools