APO1_COPRA
ID APO1_COPRA Reviewed; 261 AA.
AC B9W4V8;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Aromatic peroxygenase {ECO:0000312|EMBL:CAS12255.1};
DE Flags: Fragments;
GN Name=APO {ECO:0000312|EMBL:CAS12255.1};
OS Coprinellus radians (Coprophilous mushroom) (Coprinus radians).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinellus.
OX NCBI_TaxID=71721;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-16 AND 237-261, FUNCTION, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
RC STRAIN=ATCC 20014 / DSM 888 / 1020;
RX PubMed=17601809; DOI=10.1128/aem.00026-07;
RA Anh D.H., Ullrich R., Benndorf D., Svatos A., Muck A., Hofrichter M.;
RT "The coprophilous mushroom Coprinus radians secretes a haloperoxidase that
RT catalyzes aromatic peroxygenation.";
RL Appl. Environ. Microbiol. 73:5477-5485(2007).
RN [2] {ECO:0000312|EMBL:CAS12255.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-235, AND PROTEIN SEQUENCE OF 227-236.
RC STRAIN=ATCC 20014 / DSM 888 / 1020;
RX PubMed=19434406; DOI=10.1007/s00253-009-2000-1;
RA Pecyna M.J., Ullrich R., Bittner B., Clemens A., Scheibner K., Schubert R.,
RA Hofrichter M.;
RT "Molecular characterization of aromatic peroxygenase from Agrocybe
RT aegerita.";
RL Appl. Microbiol. Biotechnol. 84:885-897(2009).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=19039585; DOI=10.1007/s00253-008-1778-6;
RA Aranda E., Kinne M., Kluge M., Ullrich R., Hofrichter M.;
RT "Conversion of dibenzothiophene by the mushrooms Agrocybe aegerita and
RT Coprinellus radians and their extracellular peroxygenases.";
RL Appl. Microbiol. Biotechnol. 82:1057-1066(2009).
CC -!- FUNCTION: Aromatic peroxidase that oxidizes aryl alcohols into the
CC corresponding aldehydes and then into the corresponding benzoic acids.
CC Catalyzes the regioselective peroxide-dependent hydroxylation of
CC naphthalene to 1-naphthol and to a far lesser extent 2-naphthol via a
CC naphthalene 1,2-oxide intermediate. Halogenates phenol to 2-bromophenol
CC and 4-bromophenol. Oxidizes the sulfur-containing heterocycle
CC dibenzothiophene to yield sulfoxidation products, and trace amounts of
CC ring-hydroxylation products. {ECO:0000269|PubMed:17601809,
CC ECO:0000269|PubMed:19039585}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:17601809};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
CC {ECO:0000269|PubMed:17601809};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49 uM for ABTS (at pH 4.5) {ECO:0000269|PubMed:17601809};
CC KM=635 uM for benzyl alcohol (at pH 7) {ECO:0000269|PubMed:17601809};
CC KM=342 uM for dimethoxyphenol (at pH 4.5)
CC {ECO:0000269|PubMed:17601809};
CC KM=1201 uM for hydrogen peroxide (at pH 7)
CC {ECO:0000269|PubMed:17601809};
CC KM=584 uM for naphthalene (at pH 7) {ECO:0000269|PubMed:17601809};
CC KM=88 uM for veratryl alcohol (at pH 7)
CC {ECO:0000269|PubMed:17601809};
CC pH dependence:
CC Optimum pH is 5.0 with ABTS as substrate. Optimum pH is 6.0 with
CC dimethoxyphenol as substrate. Optimum pH is 8.0 with benzyl alcohol
CC as substrate, and there is another optimum at pH 4.5. Optimum pH is
CC 6.0 with naphthalene as substrate. Optimum pH is 7.0 with pyridine as
CC substrate. Optimum pH is 7.5 with veratryl alcohol as substrate, and
CC there is another optimum at pH 4.5. {ECO:0000269|PubMed:17601809};
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17601809}.
CC -!- SIMILARITY: Belongs to the chloroperoxidase family. {ECO:0000255}.
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DR EMBL; FM872459; CAS12255.1; -; mRNA.
DR SABIO-RK; B9W4V8; -.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.489.10; -; 1.
DR InterPro; IPR000028; Chloroperoxidase.
DR InterPro; IPR036851; Chloroperoxidase-like_sf.
DR Pfam; PF01328; Peroxidase_2; 1.
DR SUPFAM; SSF47571; SSF47571; 1.
DR PROSITE; PS51405; HEME_HALOPEROXIDASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN <1..>261
FT /note="Aromatic peroxygenase"
FT /id="PRO_0000391457"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04963"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14..16
FT /note="PKL -> GKK (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_CONS 236..237
FT /evidence="ECO:0000303|PubMed:17601809"
FT NON_CONS 251..252
FT /evidence="ECO:0000303|PubMed:17601809"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:17601809"
FT NON_TER 261
FT /evidence="ECO:0000303|PubMed:17601809"
SQ 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
