PERA_ALOVR
ID PERA_ALOVR Reviewed; 361 AA.
AC P84752;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 11-DEC-2019, entry version 38.
DE RecName: Full=Peroxidase A;
DE EC=1.11.1.7;
DE Flags: Fragments;
OS Aloe vera (Aloe) (Aloe barbadensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asphodelaceae;
OC Asphodeloideae; Aloe.
OX NCBI_TaxID=34199;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RC TISSUE=Leaf {ECO:0000269|Ref.1};
RA Esteban A.;
RT "Peroxidase of Aloe barbadensis m.: characterization and function.";
RL Thesis (2005), University of Alcala, Spain.
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|Ref.1};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- PTM: Partially N-glycosylated. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255}.
CC -!- CAUTION: The order of the peptides shown is unknown. {ECO:0000305}.
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DR PRIDE; P84752; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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 PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrogen peroxide; Oxidoreductase;
KW Peroxidase; Secreted.
FT CHAIN <1..>361
FT /note="Peroxidase A"
FT /id="PRO_0000055601"
FT NON_CONS 15..16
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 31..32
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 53..54
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 79..80
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 106..107
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 120..121
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 135..136
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 157..158
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 176..177
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 187..188
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 216..217
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 238..239
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 253..254
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 267..268
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 285..286
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 303..304
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 322..323
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 337..338
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 352..353
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 1
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 361
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 361 AA; 38444 MW; 4296FDD9CF88B0EE CRC64;
VNQIGSVTES IEAVKAALVS HGAGVAVVGR KINLAGGPSY TVELGRFDGL VSRALYGLSK
LPELGTHGLT LICISWALRV MSNVHDFFVH VAAKVESIHQ YIESMRYGSL SPTIFDNYSK
DCMIAHGAAH FLKXRPPDPA ETRGGAVADN GSGAVARMPT LEEYGTNLTK LAEEGKANFD
AAMVKLKNFS FILMFGVLGT IISFCLISSG AVLLLKHHVF PDSNINPSSG AAITSGVRGD
LRAYVVAYLD PSRTSFTVDN AIYGEIRRTV LAWLIDSGTL QLSEKVLALV LTMVAATVLG
VAKSMIKMGQ IEVLTGTQGE IRAAEIVVEQ LHAESGKPVL VALTGSIDKM TKDNVLNKTC
K