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Database: UniProt
Entry: B9HIL8_POPTR
LinkDB: B9HIL8_POPTR
Original site: B9HIL8_POPTR 
ID   B9HIL8_POPTR            Unreviewed;       337 AA.
AC   B9HIL8; W8Q496;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Peroxidase {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060};
DE            EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060};
GN   Name=PRX55 {ECO:0000313|EMBL:AHL39159.1};
GN   ORFNames=POPTR_008G103200 {ECO:0000313|EMBL:PNT23855.2};
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:PNT23855.2, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT23855.2, 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:PNT23855.2};
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:AHL39159.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ren L.-L.;
RT   "Functional Evolution of Populus Class III Peroxidase Gene Family.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PNT23855.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nisqually-1 {ECO:0000313|EMBL:PNT23855.2};
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   -!- 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. {ECO:0000256|ARBA:ARBA00002322}.
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}.
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DR   EMBL; KJ201820; AHL39159.1; -; mRNA.
DR   EMBL; CM009297; PNT23855.2; -; Genomic_DNA.
DR   AlphaFoldDB; B9HIL8; -.
DR   STRING; 3694.B9HIL8; -.
DR   EnsemblPlants; Potri.008G103200.1.v4.1; Potri.008G103200.1.v4.1; Potri.008G103200.v4.1.
DR   Gramene; Potri.008G103200.1.v4.1; Potri.008G103200.1.v4.1; Potri.008G103200.v4.1.
DR   eggNOG; ENOG502QTWH; Eukaryota.
DR   HOGENOM; CLU_010543_0_1_1; -.
DR   InParanoid; B9HIL8; -.
DR   OrthoDB; 1010072at2759; -.
DR   Proteomes; UP000006729; Chromosome 8.
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; PTHR31388:SF28; PEROXIDASE 40; 1.
DR   PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 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   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
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:UP000006729};
KW   Secreted {ECO:0000256|RuleBase:RU362060};
KW   Signal {ECO:0000256|RuleBase:RU362060}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT   CHAIN           19..337
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT                   /id="PRO_5033973055"
FT   DOMAIN          37..337
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   ACT_SITE        78
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         86
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         88
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT   BINDING         205
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         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         259
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         264
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   SITE            74
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT   DISULFID        47..127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        80..85
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        133..333
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        212..242
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   337 AA;  36183 MW;  166BB1A865F388C1 CRC64;
     MAMGLAICFM MLIKLVIALA KIPTTLNTTC VGDIGVLLQF DVYQESCPEA EPIILSWVQS
     AISEEPRMAA SLLRLHFHDC FVNGCDASVL LDDTENFVGE KTAPPNLNSL RGFEVIDAIK
     SDLESVCPET VSCADILAIV ARDSVLLSGG PGWEVQMGRR DSLTASKAAA TNNIPAPNSS
     VATLVANFQN VGLTQNDMVA LSGAHTMGKA RCSTFSSRFQ SPSNSGGPDV NMDFVQSLQQ
     LCSETADSTT TVAHLDLVTP ATFDNQYYVN LLSGEGLLPS DQVLVVQDDR TREIVESYAE
     DPLLFFEDFK NSMLKMGALG PLTGDSGEIR VNCRAVN
//
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