ID A0A0C3KT98_9AGAM Unreviewed; 1128 AA.
AC A0A0C3KT98;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M407DRAFT_25950 {ECO:0000313|EMBL:KIO24703.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO24703.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO24703.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO24703.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
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; KN823056; KIO24703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3KT98; -.
DR STRING; 1051891.A0A0C3KT98; -.
DR HOGENOM; CLU_002329_0_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000054248; 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; 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; 2.
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:UP000054248}.
FT BINDING 417
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 1128 AA; 124498 MW; E4CC032EFD923ED3 CRC64;
MSSTPSPLAT GKTLGNVIAD TAYSAVDSSL HAAADGVERI SDAIRAPPEA LSAEDEVDGV
YHSSLARLID SFRAQLKRGL PFELTRSNFL SIIDALLTSK LEGGLDDRLY LLEHALTFLS
RYPPGTFTSK QLQDKVISLL WYDLAHPPPS LVGSKYQFRT ADASGTSIWH PEMGKAGSPY
ARSVQTLHPL PANQLPSPEL LFDTLLKRED KVDHPAGLST FFFAFANLVI HSLFWTGVDT
SDPLKPHGDP TQPINKVSSY LDLSPLYGSS EADLKRIRLN DGTGRIHPDT FLDHRVLLMP
ASTPALLVMF SRNHNYIVEK LLNINERGKW QNPPPQDPDK KQAQDNEIFG TARLINCGWF
MSSIFGDYLA SILGLVRDGN SWSLDPLSNF RAASHEIVER GSGNIVSVEF LALYHFHSSI
GAGDAAWTEE VFEELLGTRD WDSITPTQFR IAVAKLAKDP TRPPNTPPTT WPIGKYNRVD
GKFRDEDLAK ILLDASEQSA SAFKARGTPH VMRVVEILGI QQNREWGTCS LNEFRKFLGL
KPYNTFDEWN PRKDIADAGR RLYRHPDNIE LYVGLQAEQA KTVMDGAGLC PGFTMSRAIL
ADAVALVRGD RFLTNDFTAY NLTAWGMQDC TRDPKNSANG GMMGKLLGRC LPDYFPVDSS
YTNFPFVVPS QMKEFLKKVG TADQYTFTRP VPKKRVVPLI KYYDVKNALA SPGLASTVPD
NAKIVLEGKG YLASYDTAKV NEADRKLIAE AFVPNAVVLK KHVEFLERTT EMLLQKNCYT
LVGDNKKSIN IVRDVINLLP VYFTSEHVLG LPLKTPDHPH GSALDQEVYL KFKEIYEFIF
VDIAEPCTKV AKEDTVKRHS QYFQDTVQAH IQGIASEQIP LIGLGASAIH WATQTPHESN
KWLKRLLDAG KGKSKEELAN DAMALAIAMS VELSQALTHV VDTFLGPAPG STWTPNIDGT
SLTDPSLTAH IQALAQNTSD KDATTKLAKI VVEALRTRPP VPGTYRSVVA DVAQLSKGKG
DRVYLSFTEA GVDPAVWGGG VKLTDSPPQA LFAGELVKLL GPEWLLNAVV PVVKTIFKQL
KDVKRAPGNS GQLLSFKEKI EGTPVTTYLD YKQEPTFWSS DLTVTFTS
//
