ID   Q2UKK3_ASPOR            Unreviewed;      1114 AA.
AC   Q2UKK3;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AO090003000772 {ECO:0000313|EMBL:BAE57912.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE57912.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE57912.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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DR   EMBL; AP007155; BAE57912.1; -; Genomic_DNA.
DR   RefSeq; XP_001819914.1; XM_001819862.1.
DR   AlphaFoldDB; Q2UKK3; -.
DR   STRING; 510516.Q2UKK3; -.
DR   PeroxiBase; 5333; AorLDS04.
DR   EnsemblFungi; BAE57912; BAE57912; AO090003000772.
DR   GeneID; 5991897; -.
DR   KEGG; aor:AO090003000772; -.
DR   VEuPathDB; FungiDB:AO090003000772; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000006564; Chromosome 2.
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:SF13; LINOLEATE 10R-LIPOXYGENASE; 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:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         425
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   1114 AA;  125310 MW;  7BFD5F2BE7F65EDE CRC64;
     MLRRISTNFK KSKNDRETKQ NGTQNGAQNG TQVNGDKRQS KVSPARKSAD QEPSRKAANG
     ASVFGKYAQV LHASQSPLPN QTGDGATFEQ RHGSLVQDLK SLHLEDAATL KQLSMNKIKG
     VPVDDKTMLM EKIIQIASSL PDNSENRTKA TNLFLNQLWD SLPHPPLSYV GPEYSYRSAD
     GSNNNPTLPW LGAANTPYAR SIAPLTIQPG GLPDAGLVFD SLFAREKFNP HPNKVSSLFF
     DWASLIIHDI FQTDHANPHI NKTSGYLDLS ILYGDVQEEQ DLIRTHRDGK LKPDSFSEPR
     LQAFPAACCV MLVMLNRFHN YVVEQLAEIN ENGRFTKPSP DLSEEKAKKA WAKYDEDLFQ
     TGRLITCGLY INITLYDYLR TIVNLNRVNS TWCLDPRAQM EGNDPTPSGL GNQCSVEFNL
     AYRWHSAISA NDEKWTEQIY EELMGKPAKD VTVLDLKKGL GKYAMGLSKD PSERTFAHLK
     RQEDGTFKDE ELVSILANAI EDVAGSFGAR NVPKCLRAVE IMGIEQARSW NVGSLNEFRK
     FFDLKPYERF EDINSDEEVV EALRHLYGHP DYVELYPGIV AEDAKQPMVP GVGIAPTYTI
     SRAVLSDAVA LVRGDRFYTV DYNPRNLTNW GYNEVRYDLN VNQGCVFYKL ATRAFPNWFK
     SDSIYAHYPM TIPSENRNIM KDLGRESDFS YERPSFTPPH VNLVSYPNVK LALEREEDFR
     VVWNGNTPLA SAKGGDDFWS KSLDNDQWRN SIKEFYEDIT AKLLQEKSGN LAGLKQVDIT
     RDIGNLAPVH FASKLFSLPL KTKENSRGVF TDNETFMSMA VIFTSIFFDV DKTKSFSLHH
     AARAVAEQLG HSVENHVKSI NSPSFLSGII GNRRNDHNAL KEYGDQLIKK LLESGLGVSD
     VTYSQVLPAA VAMVHNQAQM FTQIIDYYLS EGKKHLPEIN RLSKEDSKDS EDKLMRYCLE
     GFRLNGTFGS YREAQTDLSM TEETGNVNIK RGDRVFVGAV KANRDPQVFP DPNEVHLDRP
     LESYIQYGLG PHTGLGKETT LLALTSMLRV VGGLDNLRRA PGPQGELKKI HREGGYYVYL
     REDWGSYSPF PTTFKVHFDG AIPAPKKRLT YLGN
//