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Database: UniProt
Entry: A0A2I0B7E7_9ASPA
LinkDB: A0A2I0B7E7_9ASPA
Original site: A0A2I0B7E7_9ASPA 
ID   A0A2I0B7E7_9ASPA        Unreviewed;       334 AA.
AC   A0A2I0B7E7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060};
DE            EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060};
GN   Name=PER42 {ECO:0000313|EMBL:PKA63727.1};
GN   ORFNames=AXF42_Ash017011 {ECO:0000313|EMBL:PKA63727.1};
OS   Apostasia shenzhenica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Apostasioideae; Apostasia.
OX   NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA63727.1, ECO:0000313|Proteomes:UP000236161};
RN   [1] {ECO:0000313|EMBL:PKA63727.1, ECO:0000313|Proteomes:UP000236161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC   TISSUE=Stem {ECO:0000313|EMBL:PKA63727.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(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. Classical plant (class
CC       III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}.
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DR   EMBL; KZ451907; PKA63727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0B7E7; -.
DR   OrthoDB; 1010072at2759; -.
DR   Proteomes; UP000236161; 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; IPR033905; Secretory_peroxidase.
DR   PANTHER; PTHR31517; -; 1.
DR   PANTHER; PTHR31517:SF80; PEROXIDASE; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 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|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   ECO:0000313|EMBL:PKA63727.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW   Secreted {ECO:0000256|RuleBase:RU362060};
KW   Signal {ECO:0000256|RuleBase:RU362060}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT   CHAIN           25..334
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT                   /id="PRO_5013988085"
FT   DOMAIN          31..328
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT   BINDING         73
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         80
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         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT   BINDING         198
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         248
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         251
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   SITE            68
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT   DISULFID        41..120
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        74..79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        126..324
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        205..232
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   334 AA;  37463 MW;  C89AFBEFD05F1633 CRC64;
     MTASAPSLIF FFLALSALSS ICNGAESTSS GLAMNFYKES CPQAEDIIRE QVKLLYKRHK
     NTAFSWLRNL FHDCAVQSCD ASLLLDSTRK TLSEKETDRS FGMRNFRYLE DIKDAVEREC
     PGVVSCADIL VLSARDGIIA LGGPYIPLKT GRRDGKKSRS DVLEQYLPDH NESISSVLDK
     FATIGIDIPG VVALLGAHSV GRTHCVKLVH RLYPEVDPSL NPDHVPHMMK KCPDSIPDPK
     AVQYVRNDRG TPMKLDNNYY LNILDNKGLL LVDHQLAHDP RTRPFVKKMA QSQDYFFTHF
     SRAIALLSEN NPLTGEQGEV RHHCNLANRH HSDE
//
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