PER_GINBI
ID PER_GINBI Reviewed; 89 AA.
AC P85317;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Peroxidase;
DE EC=1.11.1.7;
DE Flags: Fragments;
OS Ginkgo biloba (Ginkgo) (Maidenhair tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX NCBI_TaxID=3311;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC STRAIN=PC-650; TISSUE=Callus;
RX PubMed=19055540; DOI=10.1111/j.1399-3054.2008.01185.x;
RA Novo Uzal E., Gomez Ros L.V., Pomar F., Bernal M.A., Paradela A.,
RA Albar J.P., Ros Barcelo A.;
RT "The presence of sinapyl lignin in Ginkgo biloba cell cultures changes our
RT views of the evolution of lignin biosynthesis.";
RL Physiol. Plantarum 135:196-213(2009).
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue. Active against p-coumaryl
CC alcohol, coniferyl alcohol and coniferyl aldehyde.
CC {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:19055540}.
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 Evidence={ECO:0000269|PubMed:19055540};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516,
CC ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- MASS SPECTROMETRY: Mass=32499; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19055540};
CC -!- MASS SPECTROMETRY: Mass=32818; Method=SELDI;
CC Evidence={ECO:0000269|PubMed:19055540};
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- CAUTION: The order of the peptides shown is unknown. {ECO:0000305}.
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DR PRIDE; P85317; -.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR Pfam; PF00141; peroxidase; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT CHAIN 1..>89
FT /note="Peroxidase"
FT /id="PRO_0000312874"
FT BINDING 52
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:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT UNSURE 59
FT /note="Q or K"
FT UNSURE 66
FT /note="Q or K"
FT UNSURE 69
FT /note="L or I"
FT UNSURE 75
FT /note="L or I"
FT UNSURE 76
FT /note="L or I"
FT UNSURE 78
FT /note="Q or K"
FT UNSURE 83
FT /note="F or M"
FT UNSURE 85
FT /note="L or I"
FT NON_CONS 17..18
FT /evidence="ECO:0000305"
FT NON_CONS 34..35
FT /evidence="ECO:0000305"
FT NON_CONS 43..44
FT /evidence="ECO:0000305"
FT NON_CONS 58..59
FT /evidence="ECO:0000305"
FT NON_CONS 62..63
FT /evidence="ECO:0000305"
FT NON_CONS 73..74
FT /evidence="ECO:0000305"
FT NON_CONS 80..81
FT /evidence="ECO:0000305"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_TER 89
SQ SEQUENCE 89 AA; 9406 MW; CA83C129BCB040A2 CRC64;
LSPTFYATSX PNVXXTRDSV VEIGQLADTV APVRGFDVID NIKDMVALSG SHTIGQARQA
TRSPAQVDLS NTRGLLGQAG NDFALVDDK
