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B9W4V6 (APO1_AGRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aromatic peroxygenase
Short name=AaP
EC=1.11.2.1
Gene names
Name:APO1
OrganismAgrocybe aegerita (Black poplar mushroom) (Agaricus aegerita)
Taxonomic identifier5400 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Bolbitiaceae › Agrocybe

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aromatic peroxidase that oxidizes aryl alcohols into the corresponding aldehydes and then into the corresponding benzoic acids. Oxidizes toluene and naphthalene. Catalyzes the regioselective peroxide-dependent hydroxylation of propranolol and diclofenac to 5-hydroxypropranolol and 4'-hydroxydiclofenac. Catalyzes the regioselective peroxide-dependent hydroxylation of naphthalene to 1-naphthol or 2-naphthol via a naphthalene 1,2-oxide intermediate. Catalyzes the regioselective peroxide-dependent oxidation of pyridine to pyridine N-oxide. Halogenates monochlorodimedone and phenol. Oxidizes the sulfer-containing heterocycle dibenzothiophene to yield ring-hydroxylation products and to a lesser extent sulfoxidation products. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Catalytic activity

RH + H2O2 = ROH + H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group. Ref.3

Developmental stage

Expressed at a low basal level while growing in a soybean-based medium until day 18 when expression rises significantly to peak at day 23. Expression decreases steadily after day 28 to return basal level by day 42. Ref.1 Ref.9

Post-translational modification

N-glycosylated. Ref.1 Ref.9

Sequence similarities

Belongs to the chloroperoxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=37 µM for ABTS (at pH 4.5) Ref.3 Ref.5 Ref.6

KM=1001 µM for benzyl alcohol (at pH 7) Ref.3

KM=298 µM for dimethoxyphenol (at pH 7) Ref.3

KM=1313 µM for hydrogen peroxide (at pH 7) Ref.3

KM=320 µM for naphthalene (at pH 7) Ref.5

KM=69 µM for pyridine (at pH 7) Ref.6

KM=2367 µM for veratryl alcohol (at pH 7) Ref.3

pH dependence:

Optimum pH is 4.7 with ABTS as substrate. Optimum pH is 7.2 with benzyl alcohol as substrate, and there is another optimum at pH 6.2. Optimum pH is 7.2 with dimethoxyphenol as substrate. Optimum pH is 6.0 with naphthalene as substrate. Optimum pH is 7.0 with pyridine as substrate. Optimum pH is 7.0 with veratryl alcohol as substrate, and there is another optimum at pH 5.5.

Ontologies

Keywords
   Biological processHydrogen peroxide
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheme binding

Inferred from direct assay Ref.3. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 4325 Ref.2 Ref.3
PRO_0000391456
Chain44 – 371328Aromatic peroxygenase Ref.2 Ref.3
PRO_5000442826

Sites

Metal binding791Iron (heme axial ligand) By similarity UniProtKB P04963

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Disulfide bond321 ↔ 362 Probable Ref.9

Experimental info

Sequence conflict471L → K AA sequence Ref.2
Sequence conflict471L → K AA sequence Ref.3
Sequence conflict52 – 543LEN → PEE AA sequence Ref.2
Sequence conflict52 – 543LEN → PEE AA sequence Ref.3
Sequence conflict2201I → N AA sequence Ref.2
Sequence conflict2251N → D AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
B9W4V6 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: CCD167E3958BE004

FASTA37140,652
        10         20         30         40         50         60 
MKYFPLFPTL VFAARVVAFP AYASLAGLSQ QELDAIIPTL EAREPGLPPG PLENSSAKLV 

        70         80         90        100        110        120 
NDEAHPWKPL RPGDIRGPCP GLNTLASHGY LPRNGVATPV QIINAVQEGL NFDNQAAVFA 

       130        140        150        160        170        180 
TYAAHLVDGN LITDLLSIGR KTRLTGPDPP PPASVGGLNE HGTFEGDASM TRGDAFFGNN 

       190        200        210        220        230        240 
HDFNETLFEQ LVDYSNRFGG GKYNLTVAGE LRFKRIQDSI ATNPNFSFVD FRFFTAYGET 

       250        260        270        280        290        300 
TFPANLFVDG RRDDGQLDMD AARSFFQFSR MPDDFFRAPS PRSGTGVEVV IQAHPMQPGR 

       310        320        330        340        350        360 
NVGKINSYTV DPTSSDFSTP CLMYEKFVNI TVKSLYPNPT VQLRKALNTN LDFFFQGVAA 

       370 
GCTQVFPYGR D

« Hide

References

[1]"Molecular characterization of aromatic peroxygenase from Agrocybe aegerita."
Pecyna M.J., Ullrich R., Bittner B., Clemens A., Scheibner K., Schubert R., Hofrichter M.
Appl. Microbiol. Biotechnol. 84:885-897(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
Strain: TM-A1.
[2]"The coprophilous mushroom Coprinus radians secretes a haloperoxidase that catalyzes aromatic peroxygenation."
Anh D.H., Ullrich R., Benndorf D., Svatos A., Muck A., Hofrichter M.
Appl. Environ. Microbiol. 73:5477-5485(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-57; 77-93 AND 218-232.
[3]"Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes."
Ullrich R., Nuske J., Scheibner K., Spantzel J., Hofrichter M.
Appl. Environ. Microbiol. 70:4575-4581(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-57, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: TM-A1.
[4]"The haloperoxidase of the agaric fungus Agrocybe aegerita hydroxylates toluene and naphthalene."
Ullrich R., Hofrichter M.
FEBS Lett. 579:6247-6250(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Spectrophotometric assay for detection of aromatic hydroxylation catalyzed by fungal haloperoxidase-peroxygenase."
Kluge M.G., Ullrich R., Scheibner K., Hofrichter M.
Appl. Microbiol. Biotechnol. 75:1473-1478(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita."
Ullrich R., Dolge C., Kluge M., Hofrichter M.
FEBS Lett. 582:4100-4106(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Conversion of dibenzothiophene by the mushrooms Agrocybe aegerita and Coprinellus radians and their extracellular peroxygenases."
Aranda E., Kinne M., Kluge M., Ullrich R., Hofrichter M.
Appl. Microbiol. Biotechnol. 82:1057-1066(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation."
Kluge M., Ullrich R., Dolge C., Scheibner K., Hofrichter M.
Appl. Microbiol. Biotechnol. 81:1071-1076(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Regioselective preparation of 5-hydroxypropranolol and 4'-hydroxydiclofenac with a fungal peroxygenase."
Kinne M., Poraj-Kobielska M., Aranda E., Ullrich R., Hammel K.E., Scheibner K., Hofrichter M.
Bioorg. Med. Chem. Lett. 19:3085-3087(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM872457 Genomic DNA. Translation: CAS12253.1.
FM872458 mRNA. Translation: CAS12254.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15996.
SABIO-RKB9W4V6.

Family and domain databases

Gene3D1.10.489.10. 1 hit.
InterProIPR000028. Chloroperoxidase.
[Graphical view]
PfamPF01328. Peroxidase_2. 1 hit.
[Graphical view]
SUPFAMSSF47571. Chloroperoxidase. 1 hit.
PROSITEPS51405. HEME_HALOPEROXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5472.

Entry information

Entry nameAPO1_AGRAE
AccessionPrimary (citable) accession number: B9W4V6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: March 24, 2009
Last modified: March 6, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents