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Database: UniProt
Entry: G9P0Y9_HYPAI
LinkDB: G9P0Y9_HYPAI
Original site: G9P0Y9_HYPAI 
ID   G9P0Y9_HYPAI            Unreviewed;       658 AA.
AC   G9P0Y9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Manganese lipoxygenase {ECO:0000256|ARBA:ARBA00021175};
DE            EC=1.13.11.45 {ECO:0000256|ARBA:ARBA00013178};
GN   ORFNames=TRIATDRAFT_33350 {ECO:0000313|EMBL:EHK43236.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK43236.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK43236.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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};
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:EHK43236.1}.
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DR   EMBL; ABDG02000026; EHK43236.1; -; Genomic_DNA.
DR   RefSeq; XP_013940576.1; XM_014085101.1.
DR   AlphaFoldDB; G9P0Y9; -.
DR   STRING; 452589.G9P0Y9; -.
DR   GeneID; 25783855; -.
DR   eggNOG; ENOG502QVKD; Eukaryota.
DR   HOGENOM; CLU_009802_0_0_1; -.
DR   OMA; FHNYAYA; -.
DR   OrthoDB; 1050333at2759; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          162..658
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
SQ   SEQUENCE   658 AA;  75028 MW;  D0AB3F29687A5849 CRC64;
     MEQILALVTQ LYGRVERSYN AYLDVVEVEP TWPRLLNLDQ TSEMFEWATQ VPDGKGGFME
     YPPHLKVIPN EDDVGLLKIF DKLGLLETQW IISPFIPDSW WGDIIEKGAE WVIKRIRQKT
     GDVTAWANQD PNFKALESYN ESHRKTATDV SEGRNLGLLG DWYSDRRFAE QAFTGTNPTT
     LVNIAKTPGN LLQEFIDAAE RLGYKEWHQK LTKAQSKPES LFVQDHRYFR EAFGAAPDEE
     LKHQELGAEL NWACAAVTLF ELHEDGRLHP AAIVIDYKVS MKDSVTIFNN RLEPRDPVGG
     GAAIPEEESD WPWRYAKSCA QVSDWMRHEV GVHLTRAHFI EEAVIVATRR TIRMDSIIHT
     ILAPHWYKTL SLNASARTIL VPQVIKDLVG ISPEYLQKYV LYEFENFDFV KHYVPNDLEE
     RGFPNTAEGL AAPKYKNYAY AKNMVSMWAV IRKYVSAMLL TTYKQETADA EISNDTHIQN
     WVKELRTNGR IKSFPDIKTL DALTDALTMC IHIAAPFHTA VNYLQNFYQA FVPAKPPAVC
     QKLPASLEEL KSYTEPELIN ALPIGRERQW LLAVQVPWLL SFKVADERSL IKFAYSQSRN
     YRSGFGKKAR AIRTISGQLH DDLNKLGPEF VLTSQGMDKG SIPYMVLDPN VTAVSILI
//
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