ID A0A1S3V761_VIGRR Unreviewed; 861 AA.
AC A0A1S3V761;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=LOC106772236 {ECO:0000313|RefSeq:XP_014513974.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014513974.1};
RN [1] {ECO:0000313|RefSeq:XP_014513974.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014513974.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_014513974.1; XM_014658488.2.
DR AlphaFoldDB; A0A1S3V761; -.
DR STRING; 3916.A0A1S3V761; -.
DR GeneID; 106772236; -.
DR KEGG; vra:106772236; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000087766; Chromosome 8.
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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF129; 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:UP000087766}.
FT DOMAIN 34..161
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 164..861
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 209..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 97960 MW; C47130200FFBE99E CRC64;
MFQNIVKVFA GEDKLRHRVK GTVVLMKKNV LDFNDFSASF LDNLHEFVGK RVSLQLVSAV
NVDPGNSNGL KGKLGKPAFL EDWITTIGPL TVGETAFKVT FDWDEEIGTP GAFIIRNNHH
SEFYLKSLTL EDVPGQGVIR FICNSWVYPA DKYEKDRIFF SNKTYLPSET PVPLLKYREE
ELENLRGNGK GQLQEWDRVY DYDVYNDLGN PDKGPQHARP TLGGSKEYPY PRRGRTGRPP
TKSDPKCESR LNIASSLDVY VPRDERFGHL KMADFLAYAL RSIVQVLKPE LESLFDSTPN
EFDSFEDVFK LYEGGIEVPE GILTEVRDHI PAEMLKEIFR SDGQRFLKFP VPQVIAVDKS
AWQTDEEFAR EMLAGINPVI IRGLQEFPPA SKLDPKLYGN QTSTITKEHI GSNLEGLTVD
EAIKERRLFI LDLHDAVIPY IRRINSTSTK TYASRTILFL QKNGTLKPLA IELSLPHPEG
DQYGAISKVY TPVEQGVEKS FWQLAKAYVV VVDSGYHQLI SHWLHTHAVI EPFILATNRQ
LSVLHPIHKL LQPHFRDTMN INALGRQILI NAGGALESTV CPSRYSMEFS SVLYKDWVFP
EQALPEDLVK RGVAVKDPTS PYGLRLLIED YPFASDGLEI WFAIRTWVQD YCSFYYKEND
TVKKDNELQS WWKEIREVGH GDKKNEPWWP KMQTCEDLIQ TCTILIWIAS ALHAAINFGQ
YPFGGFPPSR PAISRRFMPE KGTAEYDELV ADPVKGYLKT ISSQFQAVLG ISLVEILSKH
SSDEVYLGQR ENPYWTSDAE PLQAFEKFGK KLASIEERIL RMNSDEKFKN RFGPVKMPYT
LLYPTSKSGL TGMGVPNSIS I
//
