ID   A1D6L2_NEOFI            Unreviewed;      1118 AA.
AC   A1D6L2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Animal haem peroxidase family protein {ECO:0000313|EMBL:EAW21356.1};
GN   ORFNames=NFIA_065200 {ECO:0000313|EMBL:EAW21356.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21356.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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DR   EMBL; DS027690; EAW21356.1; -; Genomic_DNA.
DR   RefSeq; XP_001263253.1; XM_001263252.1.
DR   AlphaFoldDB; A1D6L2; -.
DR   STRING; 331117.A1D6L2; -.
DR   PeroxiBase; 5290; NfLDS03.
DR   EnsemblFungi; EAW21356; EAW21356; NFIA_065200.
DR   GeneID; 4589900; -.
DR   KEGG; nfi:NFIA_065200; -.
DR   VEuPathDB; FungiDB:NFIA_065200; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000006702; 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:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic 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   Peroxidase {ECO:0000313|EMBL:EAW21356.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         427
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   1118 AA;  126164 MW;  5E64C1887C8186BC CRC64;
     MLRRFSSTFK KKGDRESKQN GTAAAVANTN NNDNNKRHSK ISAARKSSSD DDRNEKKGDS
     VSPFEKYASV LHASRSPIPN QTGDGAYLEH EHTTSLLQDA RHLGFKDFKT LKEVIESKLP
     GGQLIDDKTM LMERIIQLVS RLPHNSKHRE ELTNAFLTEL WDSLPHPPLS YMGNDYAYRS
     ADGSNNNPTL PWLGAANTPY ARTIAPLIIQ PGGLPDPGLV FDTLFARQTF KPHPNKVSSV
     FFDWASLIIH DIFQTDYKNP NVNKTSGYLD LSILYGDVQE EQNLIRTFKD GKLKPDSFSE
     PRLQAFPATC CVLMVMLNRF HNYAVEQLAA INEDGRFTKP ADNLSEEEAK KAWAKYDEDL
     FQTGRLITCG LYINITLYDY LRTIVNLNRT NSTWCLDPRA QMEGSRTTPS GLGNQCSVEF
     NLAYRWHSAI SATDEKWTED VYERLMGKPA SEVSMTELLM GLGKYQAELP KDPSKRTFAD
     LERQADGKFK DEDLVNLLVN AVEDVAGSFG ARNVPKVLKN VEILGIIQSR KWNVGSLNEF
     RKFFGLKPYE TFEEINSDPD VAESLRSLYD HPDFVELYPG IVAEEAKQPM VPGVGIAPTY
     TISRAVLSDA VALVRGDRHY TIDYNPRNLT NWGYSEVRYD LSINQGCVFY KLATRAFPNW
     FKPDSIYAHY PMTIPSENRK IMKDLGRESH YSWDRPRYTP PRVDLVSYSN AKLVAEQQNQ
     FRAAWDDTVE FVFGKASKEF KLSQDSAFIQ KHADVMSKLL NKEEWHRSVK EFYEDITTKL
     LEDKTRRFGG LNQVDITKDV GNLAPVIFAS NVFSLPLRSK ENSRGIYTEH EMFKVLATLY
     NCLYFDIDKT KSYPLYHASQ AVGEPLGKAL EASVKALGGS SLLSGIFGSF RENNNALKEY
     GVHMTKQLLE NGLGAHEIAW AQILPTVIAM VPGQAQAFTQ IVDFYLSKEG SKHLPEIQRL
     AKQDTKESDE QLLRYCLEAV RLNDHSGLYR QSETTLAVTD EAGEVTIQPG DKVFVSFAKA
     NRDASVFPDP EEVRLDRPMN SYISPNLGPH GFLSKETSHI ALTAMLRTVG RLNNLRVAPG
     VQGQLKKIPQ PGGYSAYLRE DHGSYSVFPT TFRVQYDA
//