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Database: UniProt
Entry: A0A094AXQ3_9PEZI
LinkDB: A0A094AXQ3_9PEZI
Original site: A0A094AXQ3_9PEZI 
ID   A0A094AXQ3_9PEZI        Unreviewed;      1204 AA.
AC   A0A094AXQ3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V493_03251 {ECO:0000313|EMBL:KFY27870.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY27870.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY27870.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY27870.1}.
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DR   EMBL; JPJV01001242; KFY27870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AXQ3; -.
DR   STRING; 1420906.A0A094AXQ3; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000029327; 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; IPR001128; Cyt_P450.
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   Pfam; PF00067; p450; 1.
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:UP000029327}.
FT   REGION          75..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..106
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         508
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   1204 AA;  133563 MW;  59210B81E98178DC CRC64;
     MGITLYLADA ADSAHAAHLA KRSALLGYYQ YFTPPLYCSS TLSQAPVSPS HKPWFVCICF
     RVRICIASAL PMQPPYPTRH PVTPSPADLE SSPPNALPPM DPPPSPNQRG LRGASSVSAT
     SISSLPRPRH LSFSFLNPTL RMAPSQFKTL LGSMRRKPSH APDGKTDEQA YGKSMEEKTS
     IVHDLTHLNL THTRTVAEAI TTLASGEPMD DKDLLLEKGV SMLQTLPANS GLSQTISNKF
     IGMLWNDLPH PPPTTAGPSA RYRQPDGSGN NPWVPEMGKA GAPYSRSVPP TKPKGPNLPD
     PELVFDQLLK REGPFREHPS GLNRLFFSFA TVVIHECFQT SRTNPLINET SSYVDLSTIY
     GNNAEEQKRV RTNEQGRIFP DSLASERIML MPPGVVAVLL MFSRNHNHIV ENLLSVNEGG
     KYKDWDSLNK TEQAWQDEDL FQLTRNINVG FFASVVLKDY VAAILNTPRA NSTWSLDLGA
     EIKNGPERLE RGSGNVVSVE FAVLYHWHAA LSAADDQWME DVLRSHLPEL QSIDDVTAAD
     FKKVMMTEGH KLMATPPKEW TFGGLKRGAD GKFNDVDLAE IIKDCIEEPA HAFGAHSTPA
     SLKIVDIMGQ MQARDMFNVC TMNEFRRYLN LKPYEDFEDW NPDKETARAA ELLYGHIDNL
     ELYPGLMAEV TKPAMPGSGV CPGHTTGRGI LDDAVALVRG DRFLSYDFNS TTLTNWGFAK
     LGTVPAGAYG GMLPHLLFNA LPGAWTGTST YALLPFYTPI AAKGILKGNK VLDQYDLERP
     ASDKVVLGIH THEGCKKVFE DRENFRVMYQ AAIRKCTDGH DFMIGWDDAH RHDARSSILH
     KVFFEEGFEA NLTKFFRTNV SRLIKEKSLK YSSNRRAIDI VRDVTNVTPI LWLAERFAIP
     LKTKEQPRGL MSTPELFTIY LVLFMYQSFN IIPANEWKLR EGAMKAAPAL RAVFEAHLKT
     QQGFKEGIVD WLAKGSAFEV GPDADRLYHA LNESKLPIGD LVGDCIGMGA PVAGNLTQQA
     SLLIDLFLSE GYEEYKDRII ELSHKDDAAS ERELQGFVFE GMRHAGVVPG LPRVASKDVT
     IMDGSRGPIS IKAGHTILIA TSKAAMDPIQ FPNPEKLNPH RPFKDYILLG HGLHFCFGAR
     LVGCSLAATL KEVFKLKNIR RANGRQGHFS IVEHEFAGVK MRQYLDGNAN ESPIPTTLTL
     EYDE
//
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