ID A0A0C3D158_HEBCY Unreviewed; 1086 AA.
AC A0A0C3D158;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M413DRAFT_21993 {ECO:0000313|EMBL:KIM49871.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM49871.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM49871.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN831768; KIM49871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3D158; -.
DR STRING; 686832.A0A0C3D158; -.
DR HOGENOM; CLU_002329_0_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000053424; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000053424}.
FT BINDING 386
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 1086 AA; 120479 MW; 8DD564EB7BC0AE0F CRC64;
MAGVNPIQIL TLGADAAYLS RREPPTAPDG HYDWQVEDDG STKGGHSIIT NVIGEATILK
GKGVFVPNAK EVSGFLDLAL HPKNVDDRKD AFQAGLGIMS RLPQGSALQT DLSNAAIGML
YNVIPHPPIT FLGPEYTFRH ADGGYNNILE PDFGRAGTRY SRSAQPKRCR PSHVLPDPGL
VFDTLLRRKG FVPSQGGHAS FTFAVASLVT HQLFRTNRED WTINDTSSYL DLSVVYGHNQ
AAQDTVRDKS KGRGLLYPDT FAEERLLFLP PASSALLVLF SRNHNYIAET LLKINEKKTW
QDPPPADPQL AEKQDEEIFQ TARLVNCGHW MSVIMGDYVA GFLGVSEGNA FGLDAFSPIE
LKDGSVVTRG QGNHCSVEFN MLYRWHTTTS AVDEKWTEDA FKKAFGKPFD QITLDDFGAA
AGRVFSQAKA PKDREFGGLK RGPDGKFDDG ALANVLMSAT ENIAGQWRAN GTPPVLRIVE
IMGIEQGRKW GVCTMNEFRK FMNLKEFESF DEWNPDPTVA RAAERLYGHI DNLELYTGLQ
CESTIPTSPG LWLPAGYTMM KAVLSDAIAL VRGDRFYTSS FSPSTLTAWG YQDTKRDPNN
GGLGGAFPKL LTRHLPRHYT FNSTYTCFPF FTPEKMKASL TKQGLADKYT FTRPVPVSVP
KILNTFTGIK TVFSDPTHFK VPYGIKDPAT SGGSILDCDE KTRHDADLAL TLHAIFPTKD
SIPWLAKWYG DLVTKKIKET SWTYDGVPGR YVNIVNDVIN STAVHWAAER LCGISIKNKE
NPRGLYTEQE LWAMYAALHT LNVESFDDPE HEFSLRYAAK QAANVIVPQV AKSVVEVTPH
VATNIITRVI SQASSWIWPP TKKPCHDFLS KLSETGRPLK EIVTLVIGLC VASAVNHAHT
AVHVIDFYLD DERAKERAQI IQLIKKTDSA SVDLLHGYVR EGMRLNRQFA GLWRSAAVDA
NIVQGNGQPN VSIQAGDRIW ASFTNAHLNP AEFPNPTAID PTRPKKLYNL QGYGFHACPG
YEMSLVTIVE MVRVIFSLKN IRRAPGDAGR LRKITTIKNE TPTYQYVQTN GDLSMWPGPM
HVVYDP
//