ID A0A444G7G1_ENSVE Unreviewed; 320 AA.
AC A0A444G7G1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060};
DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060};
GN ORFNames=GW17_00004592 {ECO:0000313|EMBL:RWW30815.1};
OS Ensete ventricosum (Abyssinian banana) (Musa ensete).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Ensete.
OX NCBI_TaxID=4639 {ECO:0000313|EMBL:RWW30815.1, ECO:0000313|Proteomes:UP000288739};
RN [1] {ECO:0000313|EMBL:RWW30815.1, ECO:0000313|Proteomes:UP000288739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bedadit {ECO:0000313|Proteomes:UP000288739};
RC TISSUE=Leaf {ECO:0000313|EMBL:RWW30815.1};
RX PubMed=29896517; DOI=10.1016/j.dib.2018.03.026;
RA Yemataw Z., Muzemil S., Ambachew D., Tripathi L., Tesfaye K., Chala A.,
RA Farbos A., O'Neill P., Moore K., Grant M., Studholme D.J.;
RT "Genome sequence data from 17 accessions of Ensete ventricosum, a staple
RT food crop for millions in Ethiopia.";
RL Data Brief 18:285-293(2018).
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. {ECO:0000256|RuleBase:RU362060}.
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:0000256|ARBA:ARBA00000189,
CC ECO:0000256|RuleBase:RU362060};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC ECO:0000256|RuleBase:RU362060};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3, ECO:0000256|RuleBase:RU362060};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC ECO:0000256|RuleBase:RU362060};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWW30815.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JTFG03000265; RWW30815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444G7G1; -.
DR Proteomes; UP000288739; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR CDD; cd00693; secretory_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR PANTHER; PTHR31235:SF83; PEROXIDASE 27; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362060};
KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR600823-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR600823-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362060};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060};
KW Reference proteome {ECO:0000313|Proteomes:UP000288739};
KW Secreted {ECO:0000256|RuleBase:RU362060}.
FT DOMAIN 1..318
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 187
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 /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 35
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 8..116
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 41..75
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 122..314
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 194..226
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 320 AA; 34990 MW; A53488EAB75DEC88 CRC64;
MGFYRQSCPQ AETIVRTTVD SFFSHDPTVS APLLRLHFHD CFVRVSNTVV TAVLPLVSSS
SRTRMNRSID VKQGCDGSVL LNSTRKNLAE KDAEPNQTLD GFYVIDAAKA ALEKSCPATV
SCLEKGIAMT NESLYQVETG RRDGFVSRAS EAKAHLPSSY ANISALMANF AAKGLTAQDL
AILSGAHAIG NSHCFSFDKR LKRYRGKGGI DPTLDPHYAV KLISKCRPGN DTTTEMVPGS
STTFDTEYYE LVVKRRGLFH SDAALLHDKV TRDYVFSRLK SPEPSFFADF GSAMVKMGKV
GVLTGKAGVV RKNCALVNRW
//
