ID A0A0N1HTI0_9EURO Unreviewed; 679 AA.
AC A0A0N1HTI0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Linoleate 10R-lipoxygenase {ECO:0000313|EMBL:KPI39845.1};
GN ORFNames=AB675_3551 {ECO:0000313|EMBL:KPI39845.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI39845.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI39845.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI39845.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI39845.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFJN01000014; KPI39845.1; -; Genomic_DNA.
DR RefSeq; XP_017999808.1; XM_018143611.1.
DR AlphaFoldDB; A0A0N1HTI0; -.
DR STRING; 1664694.A0A0N1HTI0; -.
DR GeneID; 28735491; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000038010; 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: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; 1.10.640.10; 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 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:UP000038010}.
FT BINDING 382
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 679 AA; 76227 MW; 433FDF5B57BE6BA3 CRC64;
MNGASNQADV NGAANIAASN TESGHYDVAA VKGIFSQFAS LIHAAQRPLP TQTGNGSYIS
HEEPTGLLGD LGSIGWQEVK DITQILEAAA SGKPMDDRKY TMEKVIQVTA ALPEKSRARE
TLVNKFVHTL WTDLEHPPLS FLGDKFKYRS GDGSNNNYLY PQLGAAYTPY ARSVNPPPDP
FLLFDALMAR QEFTPHPSGV SSLFFAFASL VIHDCFQTDH NDFSISRTSS YVDLSTYTDH
IRLFKDGKIK PDCFSEERLL AFPPAAGVIL IMFNRFHNYV VEQLAVINEK GRFTKPSDRL
SGPSADQAWK KYDNDLFQTG RLVTCGLWVN IILKDYVRTI LNLNKTNLTW TLDPRDGLTR
ENGYGATGNQ VSAEFALCYR WHSVIGQADE VWIEKVYQQL FHKRAEEVDL RELMIGLSTF
DNDLPSDPME RSFAGLKRGA DGKFNDDELA KIMTGGAEQM AGAFGARNTP KVMRAISALA
IKQARAWNLC TLNEFRAHFG LKKCETFEEI NSDPEVAQQL RNLYEHPDYV ELYPGIMVEE
AKTPMVPGVG IAPNHTLARA ILADAIALIR GDRFYTVDYN AKNLTNWGFQ EASSDISINQ
GCVFYKLMLR AFPNNFHPDS IYAHYPFTVP EENVRVMKDL GRFDDYNFDK PVTGTHRVLL
TSYANSKYLL EHDQDFKVM
//
