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Database: UniProt
Entry: M2XQN9_GALSU
LinkDB: M2XQN9_GALSU
Original site: M2XQN9_GALSU 
ID   M2XQN9_GALSU            Unreviewed;       244 AA.
AC   M2XQN9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Peroxidase {ECO:0000313|EMBL:EME25938.1};
DE            EC=1.11.1.7 {ECO:0000313|EMBL:EME25938.1};
DE   Flags: Fragment;
GN   ORFNames=Gasu_64070 {ECO:0000313|EMBL:EME25938.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME25938.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601621-2};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR601621-
CC       2};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601621-2};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000256|PIRSR:PIRSR601621-2};
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006089}.
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DR   EMBL; KB454708; EME25938.1; -; Genomic_DNA.
DR   RefSeq; XP_005702458.1; XM_005702401.1.
DR   AlphaFoldDB; M2XQN9; -.
DR   STRING; 130081.M2XQN9; -.
DR   EnsemblPlants; EME25938; EME25938; Gasu_64070.
DR   GeneID; 17084928; -.
DR   Gramene; EME25938; EME25938; Gasu_64070.
DR   KEGG; gsl:Gasu_64070; -.
DR   OrthoDB; 168803at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.10.520.10; -; 1.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR001621; Ligninase.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356:SF66; HEME-BINDING PEROXIDASE-RELATED; 1.
DR   PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00462; LIGNINASE.
DR   PRINTS; PR00458; PEROXIDASE.
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:PIRSR601621-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Heme {ECO:0000256|PIRSR:PIRSR601621-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR601621-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601621-2};
KW   Oxidoreductase {ECO:0000313|EMBL:EME25938.1};
KW   Peroxidase {ECO:0000313|EMBL:EME25938.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT   DOMAIN          1..142
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          155..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71
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:PIRSR601621-2"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   NON_TER         244
FT                   /evidence="ECO:0000313|EMBL:EME25938.1"
SQ   SEQUENCE   244 AA;  25399 MW;  EE5B30B709C2E761 CRC64;
     SIADLINSCA VTALKFLNGP DVPVYYGRLD RNVPDPTGLI PEPTMSLSAL INAFSAIGFS
     KEDVVTLSGA HSVGVCHGIP MCPGHNTSFG NHYYQELIEG DLSGKLPTDV ELLEDNTMRS
     LVQQYANDNS QFFSDFSRVF GKYISRIHCN QTSTGPCPLD DIGNSTTSTS TSSVTSSVIP
     VVASPSSSFP SSSSPIIIGS PIVISSSSSS SSSTSSSESF PPVPPISGPF SNPPSNPGGS
     VLSV
//
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