ID O24320_PHAVU Unreviewed; 865 AA.
AC O24320;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=PHAVU_010G134900g {ECO:0000313|EMBL:ESW07500.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:AAB18970.2};
RN [1] {ECO:0000313|EMBL:AAB18970.2}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bean nodule {ECO:0000313|EMBL:AAB18970.2};
RX PubMed=10555305;
RA Porta H., Rueda-Benitez P., Campos F., Colmenero-Flores J.M.,
RA Colorado J.M., Carmona M.J., Covarrubias A.A., Rocha-Sosa M.;
RT "Analysis of lipoxygenase mRNA accumulation in the common bean (Phaseolus
RT vulgaris L.) during development and under stress conditions.";
RL Plant Cell Physiol. 40:850-858(1999).
RN [2] {ECO:0000313|EMBL:ESW07500.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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 EMBL; U76687; AAB18970.2; -; mRNA.
DR EMBL; CM002297; ESW07500.1; -; Genomic_DNA.
DR PIR; T11852; T11852.
DR RefSeq; XP_007135506.1; XM_007135444.1.
DR AlphaFoldDB; O24320; -.
DR STRING; 3885.O24320; -.
DR ProMEX; O24320; -.
DR EnsemblPlants; ESW07500; ESW07500; PHAVU_010G134900g.
DR GeneID; 18618345; -.
DR Gramene; ESW07500; ESW07500; PHAVU_010G134900g.
DR KEGG; pvu:PHAVU_010G134900g; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR OMA; NHQKAYL; -.
DR OrthoDB; 888244at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000226; Chromosome 10.
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:SF101; 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 2: Evidence at transcript level;
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:UP000000226}.
FT DOMAIN 46..173
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 176..865
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 227..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96365 MW; 5FEF687F936E760C CRC64;
MFGILGGGKG HKIKGTVVLM TKNVLDFNEV VSTAGGGVLG IAGGIFGTAN KVVGGIVDGA
TAIFSRNIAL QLVSATKTDG LGNGKVGKQT FLENHLPSLP TLGDRQDAFN ISFEWDESFG
IPGAFYIKNF MQAEFFLVSL TLEDIPNHGT IHFVCNSWVY NAKNYKKDRI FFVNKTYVPS
ETPTPLVKYR KEELENLRGD GTGQRKVSDR IYDYDVYNDL GNPDKSADLA RPVLGGSSAY
PYPRRGRTGR KASKRDPKSE APASDTYIPR DENFGHLKSS DFLTYGIKSL AQSVLPQFQS
AFGLNAEFDK FDDVRGFFEG GIHLPTDVIS NISPLPVIKE IFRTDGEQVL KFPPPHVIQV
SKSAWMTDEE FGREMLAGVN PCLIQRLQEF PPKSKLDASV YGDQTSTITK ENLEINLGGL
TVEEALNGNK LFILDHHDAF LPYLRKINDL PTAKSYATRT ILFLKDDGTL KPLAIELSLP
HPRGDEFGAV SRVILPADQG AESTIWLLAK AYVVVNDSCY HQLMSHWLNT HATIEPFVIA
TNRHLSVLHP IYKLLSPHYR DTMNINGLAR QSLINAGGII EQSFLPGPFS VEMSSAVYKS
WVFTDQALPA DLIKRGMAIE DPSSPHGLRL VIDDYPYAVD GLEIWSAIQS WVKDYVSLYY
ATDDAIKKDT ELQTWWKEAV EKGHGDLKDK PWWPKLNTPQ NLIHICSIII WTASALHAAV
NFGQYPYGGY ILNRPTLTRR LIPEPGTKEY DELSSNHQKA YLRTITGKYE AIVDLSVIEI
LSRHASDEVY LGQRDNPNWT DDTKALQAFQ KFGNKLKEIE NKILGRNNNS SLRNRVGPVK
MPYTVLLPTS KEGLTFRGIP NSISI
//
