PER_ARTRA
ID PER_ARTRA Reviewed; 364 AA.
AC P28313;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Peroxidase;
DE EC=1.11.1.7;
DE Flags: Precursor;
OS Arthromyces ramosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales.
OX NCBI_TaxID=5451;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7670182; DOI=10.1271/bbb.59.1221;
RA Sawai-Hatanaka H., Ashikari T., Tanaka Y., Asada Y., Nakayama T.,
RA Minakata H., Kunishima N., Fukuyama K., Yamada H., Shibano Y., Amachi T.;
RT "Cloning, sequencing, and heterologous expression of a gene coding for
RT Arthromyces ramosus peroxidase.";
RL Biosci. Biotechnol. Biochem. 59:1221-1228(1995).
RN [2]
RP PROTEIN SEQUENCE OF 162-186, AND GLYCOSYLATION AT ASN-163.
RX PubMed=1576150; DOI=10.1016/0167-4838(92)90244-8;
RA Kjalke M., Andersen M.B., Schneider P., Christensen B., Schuelein M.,
RA Welinder K.G.;
RT "Comparison of structure and activities of peroxidases from Coprinus
RT cinereus, Coprinus macrorhizus and Arthromyces ramosus.";
RL Biochim. Biophys. Acta 1120:248-256(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT
RP GLN-21.
RX PubMed=8289254; DOI=10.1016/s0022-2836(05)80037-3;
RA Kunishima N., Fukuyama K., Matsubara H., Hatanaka H., Shibano Y.,
RA Amachi T.;
RT "Crystal structure of the fungal peroxidase from Arthromyces ramosus at
RT 1.9-A resolution. Structural comparisons with the lignin and cytochrome c
RT peroxidases.";
RL J. Mol. Biol. 235:331-344(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=9257700; DOI=10.1016/s0014-5793(97)00751-5;
RA Itakura H., Oda Y., Fukuyama K.;
RT "Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase
RT shown by X-ray crystallographic analysis of the complex at 1.6-A
RT resolution.";
RL FEBS Lett. 412:107-110(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 36-350.
RX PubMed=10504224; DOI=10.1021/bi982925l;
RA Tsukamoto K., Itakura H., Sato K., Fukuyama K., Miura S., Takahashi S.,
RA Ikezawa H., Hosoya T.;
RT "Binding of salicylhydroxamic acid and several aromatic donor molecules to
RT Arthromyces ramosus peroxidase, investigated by X-ray crystallography,
RT optical difference spectroscopy, NMR relaxation, molecular dynamics, and
RT kinetics.";
RL Biochemistry 38:12558-12568(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-364.
RX PubMed=10915789; DOI=10.1074/jbc.m004223200;
RA Wariishi H., Nonaka D., Johjima T., Nakamura N., Naruta Y., Kubo S.,
RA Fukuyama K.;
RT "Direct binding of hydroxylamine to the heme iron of Arthromyces ramosus
RT peroxidase. Substrate analogue that inhibits compound I formation in a
RT competitive manner.";
RL J. Biol. Chem. 275:32919-32924(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; D63792; BAA09861.1; -; mRNA.
DR PIR; S22221; S22221.
DR PDB; 1ARP; X-ray; 1.90 A; A=21-364.
DR PDB; 1ARU; X-ray; 1.60 A; A=21-364.
DR PDB; 1ARV; X-ray; 1.60 A; A=21-364.
DR PDB; 1ARW; X-ray; 1.60 A; A=21-364.
DR PDB; 1ARX; X-ray; 1.90 A; A=21-364.
DR PDB; 1ARY; X-ray; 1.90 A; A=21-364.
DR PDB; 1C8I; X-ray; 2.00 A; A=21-364.
DR PDB; 1CK6; X-ray; 1.90 A; A=21-364.
DR PDB; 1GZA; X-ray; 2.06 A; A=21-364.
DR PDB; 1GZB; X-ray; 1.80 A; A=21-364.
DR PDB; 1HSR; X-ray; 1.60 A; A=21-364.
DR PDB; 2E39; X-ray; 1.30 A; A=21-364.
DR PDB; 2E3A; X-ray; 1.30 A; A=21-364.
DR PDB; 2E3B; X-ray; 1.30 A; A=21-364.
DR PDBsum; 1ARP; -.
DR PDBsum; 1ARU; -.
DR PDBsum; 1ARV; -.
DR PDBsum; 1ARW; -.
DR PDBsum; 1ARX; -.
DR PDBsum; 1ARY; -.
DR PDBsum; 1C8I; -.
DR PDBsum; 1CK6; -.
DR PDBsum; 1GZA; -.
DR PDBsum; 1GZB; -.
DR PDBsum; 1HSR; -.
DR PDBsum; 2E39; -.
DR PDBsum; 2E3A; -.
DR PDBsum; 2E3B; -.
DR AlphaFoldDB; P28313; -.
DR SMR; P28313; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; PRX2A_AGASP; -.
DR PeroxiBase; 2404; ArCIIBA.
DR iPTMnet; P28313; -.
DR BRENDA; 1.11.1.7; 462.
DR EvolutionaryTrace; P28313; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00692; ligninase; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..20
FT CHAIN 21..364
FT /note="Peroxidase"
FT /id="PRO_0000023666"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 204
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 72
FT /note="Transition state stabilizer"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8289254"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:1576150"
FT DISULFID 32..44
FT DISULFID 43..313
FT DISULFID 63..149
FT DISULFID 277..342
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:2E39"
FT TURN 56..61
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:2E39"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2E39"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1ARU"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:2E39"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2E39"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:2E39"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:2E39"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:2E39"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2E39"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2E39"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1ARP"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2E39"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1ARV"
SQ SEQUENCE 364 AA; 37746 MW; 08C3BB42B9695D88 CRC64;
MKLSLFSTFA AVIIGALALP QGPGGGGGSV TCPGGQSTSN SQCCVWFDVL DDLQTNFYQG
SKCESPVRKI LRIVFHDAIG FSPALTAAGQ FGGGGADGSI IAHSNIELAF PANGGLTDTI
EALRAVGINH GVSFGDLIQF ATAVGMSNCP GSPRLEFLTG RSNSSQPSPP SLIPGPGNTV
TAILDRMGDA GFSPDEVVDL LAAHSLASQE GLNSAIFRSP LDSTPQVFDT QFYIETLLKG
TTQPGPSLGF AEELSPFPGE FRMRSDALLA RDSRTACRWQ SMTSSNEVMG QRYRAAMAKM
SVLGFDRNAL TDCSDVIPSA VSNNAAPVIP GGLTVDDIEV SCPSEPFPEI ATASGPLPSL
APAP
