ID A0A3N7EV93_POPTR Unreviewed; 270 AA.
AC A0A3N7EV93;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN ORFNames=POPTR_003G053701 {ECO:0000313|EMBL:RQO87870.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:RQO87870.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:RQO87870.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}, and
RC Nisqually-1 {ECO:0000313|EMBL:RQO87870.1};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2] {ECO:0000313|EMBL:RQO87870.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nisqually-1 {ECO:0000313|EMBL:RQO87870.1};
RA Tuskan G., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U.,
RA Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L.,
RA Aerts A., Bhalerao R., Bhalerao R., Blaudez D., Boerjan W., Brun A.,
RA Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J.,
RA Chen G., Cooper D., Coutinho P., Couturier J., Covert S., Cronk Q.,
RA Cunningham R., Davis J., Degroeve S., Dejardin A., Depamphilis C.,
RA Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B.,
RA Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R.,
RA Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R.,
RA Joshi C., Kangasjarvi J., Karlsson J., Kelleher C., Kirkpatrick R.,
RA Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.,
RA Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C.,
RA Nelson D., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G.,
RA Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P.,
RA Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J.,
RA Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.,
RA Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G.,
RA Yin T., Douglas C., Marra M., Sandberg G., Van De Peer Y., Rokhsar D.;
RT "WGS assembly of Populus trichocarpa.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR600823-3};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
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DR EMBL; CM009292; RQO87870.1; -; Genomic_DNA.
DR EMBL; CM009292; RQO87871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N7EV93; -.
DR STRING; 3694.A0A3N7EV93; -.
DR InParanoid; A0A3N7EV93; -.
DR Proteomes; UP000006729; Chromosome 3.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR PANTHER; PTHR31235:SF292; PEROXIDASE 48-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR600823-5};
KW Iron {ECO:0000256|PIRSR:PIRSR600823-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729}.
FT DOMAIN 1..270
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 86..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 45
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 DISULFID 52..84
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 270 AA; 28790 MW; 9A3CF859ADCE2FAF CRC64;
MALFLSEILQ HIKLPSPNAD LSETLASFAS RGFDERETVS LLGGHSIGVI HCKFFQNRLY
NFSWTNKPDP SLDTGFLSLL RSRCNNNNSS KEASPSPSPS FKAPPPSSAP STSFDGTKSP
STAPSLSCSG SPSSSSSTSE MRVSPSSSTA PSPSLKGSIS SPHSSSAPSS ASFEDSLLST
LEEPGMNMAY EGPGVDFGTL YYHGLLQGKG ILYADQQLMA GVETRIWVRA YASDISLFRR
DYALAMMKLS NLRVLTGSTG QVRLHCSKVA
//
