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Database: UniProt
Entry: A0A3L6PXT0_PANMI
LinkDB: A0A3L6PXT0_PANMI
Original site: A0A3L6PXT0_PANMI 
ID   A0A3L6PXT0_PANMI        Unreviewed;       568 AA.
AC   A0A3L6PXT0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peroxidase 18-like {ECO:0000313|EMBL:RLM65319.1};
GN   ORFNames=C2845_PM16G11900 {ECO:0000313|EMBL:RLM65319.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM65319.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
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|PIRSR:PIRSR600823-3};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC       3};
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}.
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:RLM65319.1}.
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DR   EMBL; PQIB02000015; RLM65319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6PXT0; -.
DR   STRING; 4540.A0A3L6PXT0; -.
DR   Proteomes; UP000275267; Chromosome 16.
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; IEA:UniProtKB-KW.
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; PTHR31517; -; 1.
DR   PANTHER; PTHR31517:SF70; PEROXIDASE; 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   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR600823-5};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Iron {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Oxidoreductase {ECO:0000313|EMBL:RLM65319.1};
KW   Peroxidase {ECO:0000313|EMBL:RLM65319.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267}.
FT   DOMAIN          287..567
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          56..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         432
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         433
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         487
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         495
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   DISULFID        439..472
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   568 AA;  57308 MW;  90F0F021F6F36C5A CRC64;
     MTSPCRCRGV RVAPVARATY RSRWPPSDVP CRACVPTGHQ CAVCCRRAPA PFGVPRALNG
     GPAEGGRRSR DRFLPTPTCP TRRAPSLSLA PALALAACAS RAASACPLSP GGKRPFLARG
     DVPVSFRFYR SRRKDVLSLS SSAQDGAGAR RRRRLLNAGA AGAAGARRLA AGVPGSVAVS
     ERAAASAGAG REGVLPSAGS EAVAPAGAGR EAVVSTTDGA SWETISVSEA GSSAASAQRG
     ADAKAVASAC LARSTSCRAA AGPQTVSARG SGAKPFTTTC HAASAACATA GSDAATALVV
     AGAKAVAFTY HTGPTAATSS ETVSITGFTT TTTGSAAAFV ELHAVDVLDI GPALAQLLRA
     VLPGRGAGGE RCGQTGGPAV PVPLGRRDGL VSLASNVRRN IIDTGFSVDA MAASFTAKGL
     TLDDLVTLSG GHTIGSAHCN TFRERFQVAN GSMTPVDASM NTDYANELIR ACSANGAASA
     AVAVDCDSGS ASAFDNRYFA NLLEGRGLLR TDAVLVQNAT TRAKVEEFAR SQEGFFASWA
     GSYARLTSLG VKTGADGEIR RTCSSVNG
//
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