ID A0A3Q0FEC1_VIGRR Unreviewed; 1742 AA.
AC A0A3Q0FEC1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=LOC106773082 {ECO:0000313|RefSeq:XP_022642001.1};
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_022642001.1};
RN [1] {ECO:0000313|RefSeq:XP_022642001.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022642001.1};
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_022642001.1; XM_022786280.1.
DR STRING; 3916.A0A3Q0FEC1; -.
DR KEGG; vra:106773082; -.
DR OrthoDB; 917866at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000087766; Chromosome 9.
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; 2.
DR Gene3D; 3.10.450.60; -; 2.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 2.
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:SF115; SEED LINOLEATE 9S-LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 2.
DR Pfam; PF01477; PLAT; 2.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 2.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 2.
DR SUPFAM; SSF48484; Lipoxigenase; 2.
DR PROSITE; PS00711; LIPOXYGENASE_1; 2.
DR PROSITE; PS00081; LIPOXYGENASE_2; 2.
DR PROSITE; PS51393; LIPOXYGENASE_3; 2.
DR PROSITE; PS50095; PLAT; 2.
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 43..171
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 174..866
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT DOMAIN 922..1049
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 1052..1742
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 221..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1742 AA; 195233 MW; 6EF4F89258C227C5 CRC64;
MFGLFDKSQK IKGTVVLMPK NVLDANDLNA VQNGGLGGFV SGIFGAVSDV AGQVVDSATA
ILSRNVSFKL ISATSTDASG NGKVGKETYL EKHLPTLPTF GDRRDAFAVN FEWDANFGIP
GAFYIRNFMY DEFFLVSVTL DDIPNHGSIQ FVCNSWIYNF KSYKKDRIFF ANNTYVTSAT
PAPLVKYRKE ELEVLRGDGT GERKEWERIY DYDVYNDLGN PDSDKSLARP VLGGSSTHPY
PRRVRTGRKP TKKDPKSEKL AAEFYIPRDE KFGHLKSSDF LSYSLKSLSQ SLLPSLENVV
DLDFTWNEFD SFQEVRDLYE GGIKLPTGVL SDISPLPVFK ELFRSDGENV LQLPPPHVIR
VNKSAWMTDE EFAREMIAGV NPNVIRCLQE FPPKSQLDPT LYGDQTSTVT KEKLEINMGG
VTVEEALAAK RLFILDYQDA FIPYLTRINS LPTAKAYATR TILFLKDDGT LKPLAIELSK
PHPSGDNLGP VSKVVLPAID GVDSTIWLLA KAYVIVNDSG YHQLMSHWLN THAVMEPFAI
ATNRNLSVIH PIYKLLYPHY RDTININALA RQNLINANGI IEQSFLPGKY SMEMSSAVYK
NWVFTEQSLP ADLIKRGLAT EDPSAPHGLR LVIKDYPYAV DGLEIWDAIK IWVEEYVSLY
YPTDVAVQQD TELQAWWKEA VEKGHADLKD KQWWPKMKTR QELIQSSSTI IWTASALHAA
VNFGQYPYGG FILNRPTLSR RFIPEPGTKE YDEMLKSPHT AYLRTITPKR EAIIDLTVIE
ILSRHASDEI YLGKRDHPNW TSDSKALEAF KRFGSKLTEI EAKITARNTD SALKNRCGPV
ELPYTLLIPS SEEGLTFRGI PNSISITEGG KMFGIGKRTQ KIKGTVVLMP KNVLDFNAIS
SVSVPNSIGG VVGGAVGAVG GILGGVANVA GGVIDAATAF LGRNVSMQLI SATQTHGGKG
KVGEETYLNS HLPTLPTLGA RQEAFSIYFE WDSDFGIPGA FYIKNFKTDE FFLVSVTLED
IPNHGSIHFV CNSWVYNFKK YKKDRIFFVN NTYVPSATPA PLLKYRQEEL ETLRGDGTGK
RKEEDRIYDY DVYNDIGNPD GGEPRPILGG SSNYPYPRRV RSGRDKTKKD PNSEKPGEIY
VPRDENFGHL KSSDFLIYGL KSLSQNVFPL LKSAIFDLRV TSSEFDSFDD VRSLYEGGLK
LPTDILSQIS PLPALKEIFR TDGENVLQFP PPHVIRVSKS AWMTDEEFAR ETIAGVNPNV
IRRLQEFPPK SSLDPTIYGD QTSTITKEQL EINMDGVTVE EALGKDRLFI LDHHDAFIPY
LTRINNLPTS KAYATRTILF LKDDGSLKPL VIELSKTHPG GDNLGAVSKV VLPATEGVES
TIWLLAKAHV VVNDCGYHQL ISHWLNTHAV VEPFAIATNR NLSVLHPIYK LLYPHYRDTI
NINGLARQSL INADGFIEQA FLPGKYSMEI SSTVYKNWVF TDQALPADLV KRGLAVEDPS
APHGLRLLIK DYPYAVDGLE IWDAIKAWVQ DYVSLYYPTD EAIKQDTELQ AWWKEVVEKG
HGDLKDKPWW PKMHTTEDLI KSCSIIIWTA SALHAAVNYG QYPYGGYIVN RPTLTRRFIP
EPGTKEYDEM VKNPQKAYLN TITPKFESLV DISVLEILSR HASDEIYLGE RDSPYWTTDS
KALEAFKKFG SKLTEIEGKI TARNNDPSLR SRHGPVQLPY TLLLRSSEEG MTFRGIPNSI
SI
//
