ID A0A2P5HTV9_9PEZI Unreviewed; 641 AA.
AC A0A2P5HTV9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DHEL01_v207953 {ECO:0000313|EMBL:POS73655.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS73655.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS73655.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS73655.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) 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:POS73655.1}.
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DR EMBL; MAVT02000758; POS73655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5HTV9; -.
DR STRING; 158607.A0A2P5HTV9; -.
DR InParanoid; A0A2P5HTV9; -.
DR OrthoDB; 1086441at2759; -.
DR Proteomes; UP000094444; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09818; PIOX_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR034815; A_dioxygenase.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11903:SF11; ALPHA-DIOXYGENASE 1; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Reference proteome {ECO:0000313|Proteomes:UP000094444}.
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT ACT_SITE 385
FT /note="For cyclooxygenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT BINDING 388
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 641 AA; 71970 MW; B5EB8C4D90C5B423 CRC64;
MASQALGTTP RPSFLDRVGI WTFRVVNKFV PWHKLPGIVG TLQLYLFRVE LREQNLFDGY
ASTSEQGNAG DFPLPDKRFL HARHSDGTYN SLEMPLMGCA GIRFGRNFSR TATQKPSEQD
LWTPSPRVVS ERFMKRDKFI PATSLNLLAA AWIQFQIHDW FNHELSEESF DVPLEYGDAW
PGGKMRLPQT KTDKILAPSD SECPGYRNIN TGWWDGSQIY GSSEALTRQL RDHNSDGKLE
LDDKGTVAFL PRDEDGNPIT GFRDNWWVAL EMLHTLFTLE HNSICDELRK AYPSWTGDQI
FDKARLVNCA LMAKIHTVEW TPAILAHPAL KIAMNANWWG LAGETLNKLV GRISKTSEAV
SGIPGSGAAQ DGVPYSLTEE FVSVYRMHSL VPDDIAFFTA DTGKHHSTVP TVDLTFSKAQ
DPFVGPKALS FADAFYSFGI NYPGAITNHN YPDFLRNLTT PDGIPPRDLG TVDILRDRER
GVPRYNQFRR LLRLPAPKTF EELVGGVEGK DQAAKDRAAL ARDLKEVYNG DIEAVDALVG
SHSEPLPEGF GFSDTAFRIF ILMASRRLKS DRFIATQWNE ETYTPEGFKW VQNSTMRDVL
VRNLPELEHV VPPPGNNVFA PWQKLPASKS YTGKETNATV P
//
