ID A0A397V525_9GLOM Unreviewed; 325 AA.
AC A0A397V525;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 9.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:RIB16728.1};
GN ORFNames=C2G38_1487840 {ECO:0000313|EMBL:RIB16728.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB16728.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB16728.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB16728.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RIB16728.1}.
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DR EMBL; QKWP01000654; RIB16728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397V525; -.
DR STRING; 44941.A0A397V525; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
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; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11475:SF4; LD42267P; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000313|EMBL:RIB16728.1};
KW Peroxidase {ECO:0000313|EMBL:RIB16728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017307591"
FT BINDING 232
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:PIRSR619791-2"
SQ SEQUENCE 325 AA; 37245 MW; 292407A509638BA8 CRC64;
MKSKRKSSHL MTFWIDFLAF DVIKSIETGE IYNNGVLIPS DDKFYLSYGV ENTTSPPKPA
LQYNRTYSVS HGTINEATSF IDGSSIYGLN ETNLNLTLRD PVDLCKMRMN YTVDTADGKF
GYLPRGKDGQ YLIGHLPTRG GHVFTNLFHT IFIREHNRKC DELRQKYGNS LTDNEYFQEA
RKWVIALLQV VHYREYLPII MGTTLSTYTA YNSTLTPGLD YFFATATFRY GHSEASDSYQ
IMNQNGEPES ILMLENLQLP DLLEIYSVPT AVLSLSLQRQ EELDILYSDF MRAHTVGGNF
TDMASIDHLR SRDRGMPMYN DVRVN
//
