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Database: UniProt
Entry: A0A0C3D158_HEBCY
LinkDB: A0A0C3D158_HEBCY
Original site: A0A0C3D158_HEBCY 
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
//
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