ID A0A2R6W1T7_MARPO Unreviewed; 334 AA.
AC A0A2R6W1T7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060};
DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060};
GN ORFNames=MARPO_0182s0001 {ECO:0000313|EMBL:PTQ27818.1};
OS Marchantia polymorpha (Common liverwort) (Marchantia aquatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197 {ECO:0000313|EMBL:PTQ27818.1, ECO:0000313|Proteomes:UP000244005};
RN [1] {ECO:0000313|Proteomes:UP000244005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 {ECO:0000313|Proteomes:UP000244005};
RX PubMed=28985561; DOI=10.1016/j.cell.2017.09.030;
RA Bowman J.L., Kohchi T., Yamato K.T., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.S.,
RA Althoff F., Araki T., Arteaga-Vazquez M.A., Balasubrmanian S., Barry K.,
RA Bauer D., Boehm C.R., Briginshaw L., Caballero-Perez J., Catarino B.,
RA Chen F., Chiyoda S., Chovatia M., Davies K.M., Delmans M., Demura T.,
RA Dierschke T., Dolan L., Dorantes-Acosta A.E., Eklund D.M., Florent S.N.,
RA Flores-Sandoval E., Fujiyama A., Fukuzawa H., Galik B., Grimanelli D.,
RA Grimwood J., Grossniklaus U., Hamada T., Haseloff J., Hetherington A.J.,
RA Higo A., Hirakawa Y., Hundley H.N., Ikeda Y., Inoue K., Inoue S.I.,
RA Ishida S., Jia Q., Kakita M., Kanazawa T., Kawai Y., Kawashima T.,
RA Kennedy M., Kinose K., Kinoshita T., Kohara Y., Koide E., Komatsu K.,
RA Kopischke S., Kubo M., Kyozuka J., Lagercrantz U., Lin S.S., Lindquist E.,
RA Lipzen A.M., Lu C.W., De Luna E., Martienssen R.A., Minamino N.,
RA Mizutani M., Mizutani M., Mochizuki N., Monte I., Mosher R., Nagasaki H.,
RA Nakagami H., Naramoto S., Nishitani K., Ohtani M., Okamoto T., Okumura M.,
RA Phillips J., Pollak B., Reinders A., Rovekamp M., Sano R., Sawa S.,
RA Schmid M.W., Shirakawa M., Solano R., Spunde A., Suetsugu N., Sugano S.,
RA Sugiyama A., Sun R., Suzuki Y., Takenaka M., Takezawa D., Tomogane H.,
RA Tsuzuki M., Ueda T., Umeda M., Ward J.M., Watanabe Y., Yazaki K.,
RA Yokoyama R., Yoshitake Y., Yotsui I., Zachgo S., Schmutz J.;
RT "Insights into land plant evolution garnered from the Marchantia polymorpha
RT genome.";
RL Cell 171:287-304.e15(2017).
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}.
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DR EMBL; KZ772851; PTQ27818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6W1T7; -.
DR EnsemblPlants; PTQ27818; PTQ27818; MARPO_0182s0001.
DR Gramene; PTQ27818; PTQ27818; MARPO_0182s0001.
DR Proteomes; UP000244005; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
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:0004601; F:peroxidase activity; IBA:GO_Central.
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; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235:SF399; PEROXIDASE; 1.
DR PANTHER; PTHR31235; PEROXIDASE 25-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; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5}; Heme {ECO:0000256|RuleBase:RU362060};
KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060};
KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3,
KW ECO:0000256|RuleBase:RU362060};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362060};
KW Peroxidase {ECO:0000256|RuleBase:RU362060};
KW Reference proteome {ECO:0000313|Proteomes:UP000244005};
KW Secreted {ECO:0000256|RuleBase:RU362060};
KW Signal {ECO:0000256|RuleBase:RU362060}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT CHAIN 28..334
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT /id="PRO_5015212346"
FT DOMAIN 34..334
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
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 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 201
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 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 44..123
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 77..82
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 129..330
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 208..243
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 334 AA; 35683 MW; B81F5DD8DBFDBA5E CRC64;
MATASANGPN ALLVSVVLLA TVCACSALSP YAAGLSEDFY HKSCPQAASI VDAYVTKFLK
KDRNFAGAFN RLQFHDCWVG GCDGSVLLNS TETNQAEREA HVNFGLRGVA EIDEIKAALE
HLCPGVVSCA DILILAARDA TAKVGGPTWT VALGRRDGVN STALMADTNL PFPVLNFSGL
VANFAAKGFG AREMITLSGA HTIGRSHCNG ILPHLYNFTG RDDATDTDPA MNKNFAVFLK
KLCPEGNRTN TIFIDSTANT FDRAYYKNVL QGKGIFITDS TLITNPVGKK VVTTFSKPRS
SFFTEFAAGM VKMGNLGVLT GTEGEIRKTC QFVN
//
