ID A0A165EAI8_9APHY Unreviewed; 1003 AA.
AC A0A165EAI8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:KZT06596.1};
GN ORFNames=LAESUDRAFT_812590 {ECO:0000313|EMBL:KZT06596.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT06596.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT06596.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT06596.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427623; KZT06596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EAI8; -.
DR STRING; 1314785.A0A165EAI8; -.
DR InParanoid; A0A165EAI8; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000076871; 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:UniProtKB-KW.
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; 1.10.640.10; 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 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; 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:0000313|EMBL:KZT06596.1};
KW Peroxidase {ECO:0000313|EMBL:KZT06596.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT BINDING 387
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 1003 AA; 112831 MW; 75DE98A87A0DA505 CRC64;
MKTNAILSPR KDTDDYIVGV NAPFDPYGVR SADRSLTRSV RDVVQNLMRF RFFSLADIRA
ILNVAQNILG HGPGIDDRLY FLERLLIFIA RSPDNFAIAR NLQLDVINIL FKDLQSPPVN
FLAIPSVVPS PIEFVNYAYR TADGSNYNVL MPTLGMAGSP YVRSVPGTTP IPQHHLPEPE
LVFNMLLRRD GFVEHPGGLS SLFFSFANLI IHSIFHTNPR DWTINDASSY LDLSPLYGSN
QEQVDSVRRK DGTGRLWEDV FADARLLLMP PSTGALLVLF CRNHNYVAER IRAINEFRTY
ADPATLDEKG RAAQDDEIFQ RARLVNTAFF MQVILGDYVG AILGLTRDGL TWRLDPLQAM
REPTHEWIPR GDGNVVSIEF NLMYRWHMAI SKEDRDWTDD LFHQMFPGMD FDQITVEDFW
KAVREYRERL PTDLREWTFS GLQRDASGRY NDADLAHILQ SATEAPAGAF RARGIPEALR
VVEILGILQA RSWGTCSLNE FRSFMGLRPY RSFKEWNPDP KVYMAAEKLY HNIDNLELYV
GMQAEETKVP MPGAGLCPGF TMSRAILADA VCLTRGDRFL TVDLTPFNLT TWGFQDVQVN
GLDGSCGGIL SRLLIRTLPA CYSASSAYTL FPFMVPKRMK EYVTKWPGSP VDQYLWTRQE
SLTNGIRKEL GVEKMAQRIL GVLPDRQSVH KALYEPGALE RHAASFGKIT RSLIVAKSVV
HANLAMRYVN VVKDVVNLIP VYWIAKYATG IPMKTEANPQ GFFGEQELVH MFADVASYLS
PDINTSEEFE LREKYLKIAQ VVTDVVKFHL SQFESGSPLG TPGRAADHYE HDRKFLTALR
ASGKHAGYDA LAAGVFVEIV ASAAPYSRAL AHVVDYFLEE GEREELVRWL AAGKEGEAQV
EEGIFRALGS DQTNGVPKSN GISHSALLLN KQGLVKPIFF VKTAAEVLRA IFALDGLRRV
PGVKGILNQL SDSMDGRQEH FYLDTEGKVT EWPVSMTVQY IVH
//
