ID A0A093VY48_TALMA Unreviewed; 663 AA.
AC A0A093VY48;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Linoleate 10R-lipoxygenase {ECO:0000313|EMBL:KFX51541.1};
GN ORFNames=GQ26_0052970 {ECO:0000313|EMBL:KFX51541.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX51541.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX51541.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX51541.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX51541.1}.
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DR EMBL; JPOX01000005; KFX51541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VY48; -.
DR HOGENOM; CLU_002329_2_1_1; -.
DR Proteomes; UP000029285; 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; 2.
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:0000256|ARBA:ARBA00022964}.
FT BINDING 378
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 663 AA; 75412 MW; 883197D2CB20AEB3 CRC64;
MESAAQFLGD IATNSKVILK GTKDHVDGII ADLHAVGLKT TAEDAQSLAT YLAQMKTGDG
VDDRAMRQEK LMSWLFKLPL EPKSAVGSTL EHGVVQSLWD TLPNPCPGWT QHSGPQYRRA
DGSFNNLYEP RVGRAGEAYI RNVVSLRDQS KDLPSPEDVF EKLFRRRTPA DGGFRKHPCG
ISANMFYMAT LITHDLFNTD ITNRFRNKTT SYVDMAWLYG KFHDVRWNQE MQDSVRDKAG
HCGKLHADVF ADPRLDLQPP GVIAMALLWC RNHNWIAEQL LIESKDDPRF SAVPKNDDQQ
GLELLDEHLF QTARNINVGT FATVVLKDYV RMLLGINREN TTWTLPINQE FSPSTKNDIP
KATGNQCSIE FNFIYRWHSA ISVEDEQWIE GLFEDLEKRL GPNWMNNRLG SILPARIPAF
VQERHDERAS TDPRCRTYFA LNPEVKRDPK THKYPDAALA DFIKRATESS AGAFGGRQVP
NVFKDIEIMS IRHARELGVC TLNELRTLCN LRPYRTFSEM NDNEAIATAL KDLYGDIADV
ELYRGLVAEQ AKPRQEATGL CAGRTITYVI LSDAVALVRG DRFLTTELNP YNLTKWGYDE
IQPDNSWSFG NVLGDKLLNR HLGEENMPRD SIYTQYMFST PEETTRNIKR FGMEKVYRDE
ALI
//
