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Database: UniProt
Entry: A0A445I0W5_GLYSO
LinkDB: A0A445I0W5_GLYSO
Original site: A0A445I0W5_GLYSO 
ID   A0A445I0W5_GLYSO        Unreviewed;       901 AA.
AC   A0A445I0W5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN   ORFNames=D0Y65_029797 {ECO:0000313|EMBL:RZB79715.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB79715.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZB79715.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB79715.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC       aspects of plant physiology including growth and development, pest
CC       resistance, and senescence or responses to wounding.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|RuleBase:RU003974};
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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:RZB79715.1}.
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DR   EMBL; QZWG01000011; RZB79715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445I0W5; -.
DR   SMR; A0A445I0W5; -.
DR   OrthoDB; 462210at2759; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000289340; Chromosome 11.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01751; PLAT_LH2; 1.
DR   Gene3D; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR036226; LipOase_C_sf.
DR   InterPro; IPR020834; LipOase_CS.
DR   InterPro; IPR020833; LipOase_Fe_BS.
DR   InterPro; IPR001246; LipOase_plant.
DR   InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR   InterPro; IPR027433; Lipoxygenase_dom_3.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR11771:SF194; LINOLEATE 13S-LIPOXYGENASE 2-1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00468; PLTLPOXGNASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|RuleBase:RU003975};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU003975};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW   ECO:0000256|RuleBase:RU003975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340}.
FT   DOMAIN          88..208
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          211..901
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   REGION          257..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  102628 MW;  81A4FFD579C291A4 CRC64;
     MLMQQVHVSN PSSSCLILQK PCLRDITHPS FQLWSRPSSF PNQRKQKRVS YGCRSNGNKI
     KAVAVTEAEN KSVKVKATIT VQPTVGGIFS EMAIERGLDD IKDLLGQSIL LELASTELDP
     KTKLEKETIK DYAHSKHRSA QEVKYEGEFE VPDNFGEVGA IFVTNEHHRE MFIKDIVLDG
     FLLGPVKFTC ESWVHSKYDN PAKRVFFSNK SYLPSETPEG VKRLREEELE QLRGNGQGER
     KSFERIYDYD VYNDLGDPDS SDDLKRPVLG GNQHPYPRRC RTGRPRCDKD PLSEKRSSTV
     YVPRDESFSE VKQLTFSTKT LSSGLKALVP ALKTLIVDKN LGFPVFSAID DLFDEGLYLP
     PLKGIRSILP RLVRHIKDIQ EDILLFDPPA TMNKDRFFWL RDEEFGRQTL AGLNPCCIQL
     VTEWPLKSKL DPEIYGPAES AITTEIVERE IRGFNTVEEA IKQKKLFILD YHDLLLPLVK
     DVRELEGTTL YGSRALFFLT REGTLRPLAI ELTRPPMDGK PQWKEVFTPC WHSTGVWLWR
     LAKLHILAHD SGYHQLVSHW LRTHCATEPY ILATNRQLSA MHPIYRLLHP HFRYTMEINA
     LAREALINGD GIIESSFSPG KHSILLSSIA YDQQWQFDLQ SLPKDLISRG MAVEDPTAPH
     GLKLIIEDYP YANDGLVLWD ALKTWFTEYV NLYYADDGSI VSDTELQAWW EEIRTVGHGD
     KKDEPWWPVL KTKLDLIDIV TTIAWTTSGH HAAVNFGQFS FAGYFPNRPT IARNNMPSED
     PSDAEWELFL EKPEVIMLKC FPSQIQATTV MTVLDILSNH SPDEEYLGET VEPAWEEEPL
     VKAAFEKFRG KLIELEGIID ARNADRTRRN RNGAGIVPYE LLKPSSEPGV TGKGVPYSIS
     I
//
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