ID A0A2T3ZL74_9HYPO Unreviewed; 658 AA.
AC A0A2T3ZL74;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Manganese lipoxygenase {ECO:0000256|ARBA:ARBA00021175};
DE EC=1.13.11.45 {ECO:0000256|ARBA:ARBA00013178};
GN ORFNames=M441DRAFT_130828 {ECO:0000313|EMBL:PTB45533.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB45533.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB45533.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB45533.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:18993, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57467; EC=1.13.11.45;
CC Evidence={ECO:0000256|ARBA:ARBA00000366};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; KZ679257; PTB45533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZL74; -.
DR STRING; 1042311.A0A2T3ZL74; -.
DR OrthoDB; 1050333at2759; -.
DR Proteomes; UP000240493; Unassembled WGS sequence.
DR GO; GO:0050584; F:linoleate 11-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:UniProt.
DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR Gene3D; 3.10.450.60; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF153; LIPOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 162..658
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 658 AA; 74968 MW; 416BAE6EDC211077 CRC64;
MEQILALVTQ LYGRVERSYN AYLDVVEVEP TWPRLLNLDQ TSEMFEWSTQ VPDGNGGFLE
YPPHLKVIPS EDDVGLFKIF DKLGLMETQW IISPFIPDSW WGGIVEKGAE WIIKRIRQKT
GDVTAWANQD PNFKALESYN ESNRKAATDV AEGRNIGLLG DWYSDRRFAE QAFTGTNPTT
LVNIAKTPGN LLQEFIDTAE RKGYKKWHER LSKAQSNPES LFVQDHRHFR EAFGAASDEE
LKHQEPGSEL NWACAAVTLF ELHEDGRLHP VAIVIDYKIS MEKSVTIFNH RLEPREPVGT
GAAIPEEESD WPWRYAKSCA QVSDWMRHEV GVHLTRAHFI EEAIIVATRR TIRMDSIIHT
ILSPHWYKTL SLNAAARTTL VPQVIKDLVG ISPTYLQKYV LYEFENFDFV KHYVPNDLKE
RGFPNTAEGL AAPKYKNYAY AKNMVSMWAV IRKYVSAMLL TTYDKDTADA DISKDTHIQN
WVNEIRTSGR IKSFPDITTL DALTDALTMC IHIAAPFHTA VNYLQNFYQA FVPAKPPAVC
TKLPASLEEL QGYTEPELIN ALPIGRERQW LLAVQVPWLL SFKVADERSL LKFAYSQSRN
YRSGWSKKAK AIRTISGQLH DDLKELGTEF VLTSQAMDKG SIPYMVMDPN VTAVSILI
//