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Aromatic peroxygenase (Fragments)

 APO1_COPRA              Reviewed;         261 AA.
B9W4V8;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 2.
25-OCT-2017, entry version 21.
RecName: Full=Aromatic peroxygenase {ECO:0000312|EMBL:CAS12255.1};
Flags: Fragments;
Name=APO {ECO:0000312|EMBL:CAS12255.1};
Coprinellus radians (Coprophilous mushroom) (Coprinus radians).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
Coprinellus.
NCBI_TaxID=71721;
[1] {ECO:0000305}
PROTEIN SEQUENCE OF 1-16 AND 237-261, FUNCTION, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
STRAIN=ATCC 20014 / DSM 888 / 1020;
PubMed=17601809; DOI=10.1128/AEM.00026-07;
Anh D.H., Ullrich R., Benndorf D., Svatos A., Muck A., Hofrichter M.;
"The coprophilous mushroom Coprinus radians secretes a haloperoxidase
that catalyzes aromatic peroxygenation.";
Appl. Environ. Microbiol. 73:5477-5485(2007).
[2] {ECO:0000312|EMBL:CAS12255.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 7-235, AND PROTEIN SEQUENCE OF 227-236.
STRAIN=ATCC 20014 / DSM 888 / 1020;
PubMed=19434406; DOI=10.1007/s00253-009-2000-1;
Pecyna M.J., Ullrich R., Bittner B., Clemens A., Scheibner K.,
Schubert R., Hofrichter M.;
"Molecular characterization of aromatic peroxygenase from Agrocybe
aegerita.";
Appl. Microbiol. Biotechnol. 84:885-897(2009).
[3] {ECO:0000305}
FUNCTION.
PubMed=19039585; DOI=10.1007/s00253-008-1778-6;
Aranda E., Kinne M., Kluge M., Ullrich R., Hofrichter M.;
"Conversion of dibenzothiophene by the mushrooms Agrocybe aegerita and
Coprinellus radians and their extracellular peroxygenases.";
Appl. Microbiol. Biotechnol. 82:1057-1066(2009).
-!- FUNCTION: Aromatic peroxidase that oxidizes aryl alcohols into the
corresponding aldehydes and then into the corresponding benzoic
acids. Catalyzes the regioselective peroxide-dependent
hydroxylation of naphthalene to 1-naphthol and to a far lesser
extent 2-naphthol via a naphthalene 1,2-oxide intermediate.
Halogenates phenol to 2-bromophenol and 4-bromophenol. Oxidizes
the sulfur-containing heterocycle dibenzothiophene to yield
sulfoxidation products, and trace amounts of ring-hydroxylation
products. {ECO:0000269|PubMed:17601809,
ECO:0000269|PubMed:19039585}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:17601809};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
{ECO:0000269|PubMed:17601809};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=49 uM for ABTS (at pH 4.5) {ECO:0000269|PubMed:17601809};
KM=635 uM for benzyl alcohol (at pH 7)
{ECO:0000269|PubMed:17601809};
KM=342 uM for dimethoxyphenol (at pH 4.5)
{ECO:0000269|PubMed:17601809};
KM=1201 uM for hydrogen peroxide (at pH 7)
{ECO:0000269|PubMed:17601809};
KM=584 uM for naphthalene (at pH 7)
{ECO:0000269|PubMed:17601809};
KM=88 uM for veratryl alcohol (at pH 7)
{ECO:0000269|PubMed:17601809};
pH dependence:
Optimum pH is 5.0 with ABTS as substrate. Optimum pH is 6.0 with
dimethoxyphenol as substrate. Optimum pH is 8.0 with benzyl
alcohol as substrate, and there is another optimum at pH 4.5.
Optimum pH is 6.0 with naphthalene as substrate. Optimum pH is
7.0 with pyridine as substrate. Optimum pH is 7.5 with veratryl
alcohol as substrate, and there is another optimum at pH 4.5.
{ECO:0000269|PubMed:17601809};
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:17601809}.
-!- SIMILARITY: Belongs to the chloroperoxidase family. {ECO:0000255}.
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EMBL; FM872459; CAS12255.1; -; mRNA.
SABIO-RK; B9W4V8; -.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
Gene3D; 1.10.489.10; -; 1.
InterPro; IPR000028; Chloroperoxidase.
InterPro; IPR036851; Chloroperoxidase_sf.
Pfam; PF01328; Peroxidase_2; 1.
SUPFAM; SSF47571; SSF47571; 1.
PROSITE; PS51405; HEME_HALOPEROXIDASE; 1.
1: Evidence at protein level;
Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide;
Iron; Metal-binding; Oxidoreductase; Peroxidase.
CHAIN <1 >261 Aromatic peroxygenase.
/FTId=PRO_0000391457.
METAL 36 36 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P04963}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 14 16 PKL -> GKK (in Ref. 1; AA sequence).
{ECO:0000305}.
NON_CONS 236 237 {ECO:0000303|PubMed:17601809}.
NON_CONS 251 252 {ECO:0000303|PubMed:17601809}.
NON_TER 1 1 {ECO:0000303|PubMed:17601809}.
NON_TER 261 261 {ECO:0000303|PubMed:17601809}.
SEQUENCE 261 AA; 28641 MW; CAF51E5E1F2148A9 CRC64;
VPGGLXPPPE YVGPKLVNDA DHPWEPLRPG DIRGPCPGLN TLASHGYLPR NGVATPAQII
NAIVEGFNFN YEGAVFVTYF AHIVDGNLVT DLLSIGGKTN LTGEDTGAPA IIGGLNTHSV
FEGDASMTRD DFHFGDNHSF NQTLFDQFVE YSNTYGGGFY NQEVAGHLRR RRIEQSIATN
PEFDFTSPRF FTAFAESSFP YSFFVDGRIT ERPGGLSMEN ATLFFRDHKM PDDFWRNVNG
EMTFTGTPDP NSAPSNLALG H


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