APO1_AGRAE
ID APO1_AGRAE Reviewed; 371 AA.
AC B9W4V6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Aromatic peroxygenase {ECO:0000303|PubMed:15294788, ECO:0000303|PubMed:16253244, ECO:0000303|PubMed:17410351, ECO:0000303|PubMed:18815784, ECO:0000303|PubMed:19022254, ECO:0000303|PubMed:19039585, ECO:0000303|PubMed:19394224};
DE Short=AaP {ECO:0000303|PubMed:15294788};
DE EC=1.11.2.1;
DE Flags: Precursor;
GN Name=APO1 {ECO:0000312|EMBL:CAS12253.1};
OS Agrocybe aegerita (Black poplar mushroom) (Agaricus aegerita).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Bolbitiaceae; Cyclocybe.
OX NCBI_TaxID=1973307;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAS12253.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=TM-A1 {ECO:0000312|EMBL:CAS12253.1};
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 [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 44-57; 77-93 AND 218-232.
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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 44-57, FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=TM-A1 {ECO:0000269|PubMed:15294788};
RX PubMed=15294788; DOI=10.1128/aem.70.8.4575-4581.2004;
RA Ullrich R., Nuske J., Scheibner K., Spantzel J., Hofrichter M.;
RT "Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita
RT oxidizes aryl alcohols and aldehydes.";
RL Appl. Environ. Microbiol. 70:4575-4581(2004).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=16253244; DOI=10.1016/j.febslet.2005.10.014;
RA Ullrich R., Hofrichter M.;
RT "The haloperoxidase of the agaric fungus Agrocybe aegerita hydroxylates
RT toluene and naphthalene.";
RL FEBS Lett. 579:6247-6250(2005).
RN [5] {ECO:0000305}
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17410351; DOI=10.1007/s00253-007-0942-8;
RA Kluge M.G., Ullrich R., Scheibner K., Hofrichter M.;
RT "Spectrophotometric assay for detection of aromatic hydroxylation catalyzed
RT by fungal haloperoxidase-peroxygenase.";
RL Appl. Microbiol. Biotechnol. 75:1473-1478(2007).
RN [6] {ECO:0000305}
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19022254; DOI=10.1016/j.febslet.2008.11.006;
RA Ullrich R., Dolge C., Kluge M., Hofrichter M.;
RT "Pyridine as novel substrate for regioselective oxygenation with aromatic
RT peroxygenase from Agrocybe aegerita.";
RL FEBS Lett. 582:4100-4106(2008).
RN [7] {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).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=18815784; DOI=10.1007/s00253-008-1704-y;
RA Kluge M., Ullrich R., Dolge C., Scheibner K., Hofrichter M.;
RT "Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe
RT aegerita proceeds via oxygen transfer from H2O2 and intermediary
RT epoxidation.";
RL Appl. Microbiol. Biotechnol. 81:1071-1076(2009).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=19394224; DOI=10.1016/j.bmcl.2009.04.015;
RA Kinne M., Poraj-Kobielska M., Aranda E., Ullrich R., Hammel K.E.,
RA Scheibner K., Hofrichter M.;
RT "Regioselective preparation of 5-hydroxypropranolol and 4'-
RT hydroxydiclofenac with a fungal peroxygenase.";
RL Bioorg. Med. Chem. Lett. 19:3085-3087(2009).
CC -!- FUNCTION: Aromatic peroxidase that oxidizes aryl alcohols into the
CC corresponding aldehydes and then into the corresponding benzoic acids.
CC Oxidizes toluene and naphthalene. Catalyzes the regioselective
CC peroxide-dependent hydroxylation of propranolol and diclofenac to 5-
CC hydroxypropranolol and 4'-hydroxydiclofenac. Catalyzes the
CC regioselective peroxide-dependent hydroxylation of naphthalene to 1-
CC naphthol or 2-naphthol via a naphthalene 1,2-oxide intermediate.
CC Catalyzes the regioselective peroxide-dependent oxidation of pyridine
CC to pyridine N-oxide. Halogenates monochlorodimedone and phenol.
CC Oxidizes the sulfur-containing heterocycle dibenzothiophene to yield
CC ring-hydroxylation products and to a lesser extent sulfoxidation
CC products. {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:16253244,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:18815784,
CC ECO:0000269|PubMed:19022254, ECO:0000269|PubMed:19039585,
CC ECO:0000269|PubMed:19394224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + H2O2 = ROH + H2O.; EC=1.11.2.1;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:15294788};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
CC {ECO:0000269|PubMed:15294788};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for ABTS (at pH 4.5) {ECO:0000269|PubMed:15294788,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254};
CC KM=1001 uM for benzyl alcohol (at pH 7) {ECO:0000269|PubMed:15294788,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254};
CC KM=298 uM for dimethoxyphenol (at pH 7) {ECO:0000269|PubMed:15294788,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254};
CC KM=1313 uM for hydrogen peroxide (at pH 7)
CC {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351,
CC ECO:0000269|PubMed:19022254};
CC KM=320 uM for naphthalene (at pH 7) {ECO:0000269|PubMed:15294788,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254};
CC KM=69 uM for pyridine (at pH 7) {ECO:0000269|PubMed:15294788,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254};
CC KM=2367 uM for veratryl alcohol (at pH 7)
CC {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351,
CC ECO:0000269|PubMed:19022254};
CC pH dependence:
CC Optimum pH is 4.7 with ABTS as substrate. Optimum pH is 7.2 with
CC benzyl alcohol as substrate, and there is another optimum at pH 6.2.
CC Optimum pH is 7.2 with dimethoxyphenol as substrate. Optimum pH is
CC 6.0 with naphthalene as substrate. Optimum pH is 7.0 with pyridine as
CC substrate. Optimum pH is 7.0 with veratryl alcohol as substrate, and
CC there is another optimum at pH 5.5. {ECO:0000269|PubMed:15294788,
CC ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254};
CC -!- DEVELOPMENTAL STAGE: Expressed at a low basal level while growing in a
CC soybean-based medium until day 18 when expression rises significantly
CC to peak at day 23. Expression decreases steadily after day 28 to return
CC basal level by day 42. {ECO:0000269|PubMed:19434406}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19434406}.
CC -!- SIMILARITY: Belongs to the chloroperoxidase family. {ECO:0000255}.
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DR EMBL; FM872457; CAS12253.1; -; Genomic_DNA.
DR EMBL; FM872458; CAS12254.1; -; mRNA.
DR PDB; 2YOR; X-ray; 2.19 A; A/B=47-371.
DR PDB; 2YP1; X-ray; 2.31 A; A/B/C/D=47-371.
DR PDB; 5OXT; X-ray; 1.42 A; A/B/C=44-371.
DR PDB; 5OXU; X-ray; 1.47 A; A=44-371.
DR PDB; 5OY1; X-ray; 1.43 A; A=44-371.
DR PDB; 5OY2; X-ray; 1.36 A; A=44-371.
DR PDB; 6EKW; X-ray; 1.43 A; A=44-371.
DR PDB; 6EKX; X-ray; 1.13 A; A=44-371.
DR PDB; 6EKY; X-ray; 1.23 A; A=44-371.
DR PDB; 6EKZ; X-ray; 1.08 A; A=44-371.
DR PDB; 6EL0; X-ray; 1.65 A; A=44-371.
DR PDB; 6EL4; X-ray; 1.53 A; A=44-371.
DR PDBsum; 2YOR; -.
DR PDBsum; 2YP1; -.
DR PDBsum; 5OXT; -.
DR PDBsum; 5OXU; -.
DR PDBsum; 5OY1; -.
DR PDBsum; 5OY2; -.
DR PDBsum; 6EKW; -.
DR PDBsum; 6EKX; -.
DR PDBsum; 6EKY; -.
DR PDBsum; 6EKZ; -.
DR PDBsum; 6EL0; -.
DR PDBsum; 6EL4; -.
DR AlphaFoldDB; B9W4V6; -.
DR SMR; B9W4V6; -.
DR ChEMBL; CHEMBL5472; -.
DR KEGG; ag:CAS12253; -.
DR BioCyc; MetaCyc:MON-15996; -.
DR BRENDA; 1.11.2.1; 8897.
DR SABIO-RK; B9W4V6; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..43
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15294788,
FT ECO:0000269|PubMed:17601809"
FT /id="PRO_0000391456"
FT CHAIN 44..371
FT /note="Aromatic peroxygenase"
FT /evidence="ECO:0000269|PubMed:15294788,
FT ECO:0000269|PubMed:17601809"
FT /id="PRO_5000442826"
FT BINDING 79
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 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..362
FT /evidence="ECO:0000269|PubMed:19434406"
FT CONFLICT 47
FT /note="L -> K (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..54
FT /note="LEN -> PEE (in Ref. 2; AA sequence and 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:6EKZ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:6EKZ"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:6EKZ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6EKZ"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6EKZ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6EKZ"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 205..222
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:6EKZ"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:6EKZ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:6EKZ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6EKZ"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:6EKZ"
SQ SEQUENCE 371 AA; 40652 MW; CCD167E3958BE004 CRC64;
MKYFPLFPTL VFAARVVAFP AYASLAGLSQ QELDAIIPTL EAREPGLPPG PLENSSAKLV
NDEAHPWKPL RPGDIRGPCP GLNTLASHGY LPRNGVATPV QIINAVQEGL NFDNQAAVFA
TYAAHLVDGN LITDLLSIGR KTRLTGPDPP PPASVGGLNE HGTFEGDASM TRGDAFFGNN
HDFNETLFEQ LVDYSNRFGG GKYNLTVAGE LRFKRIQDSI ATNPNFSFVD FRFFTAYGET
TFPANLFVDG RRDDGQLDMD AARSFFQFSR MPDDFFRAPS PRSGTGVEVV IQAHPMQPGR
NVGKINSYTV DPTSSDFSTP CLMYEKFVNI TVKSLYPNPT VQLRKALNTN LDFFFQGVAA
GCTQVFPYGR D
