ID F6HB91_VITVI Unreviewed; 903 AA.
AC F6HB91;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN OrderedLocusNames=VIT_13s0064g01480 {ECO:0000313|EMBL:CCB49475.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB49475.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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 -!- 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; FN595509; CCB49475.1; -; Genomic_DNA.
DR RefSeq; XP_002263854.1; XM_002263818.3.
DR AlphaFoldDB; F6HB91; -.
DR STRING; 29760.F6HB91; -.
DR PaxDb; 29760-VIT_13s0064g01480-t01; -.
DR EnsemblPlants; Vitvi00g04467_t001; Vitvi00g04467_P001; Vitvi00g04467.
DR EnsemblPlants; Vitvi14g04489_t001; Vitvi14g04489_P001; Vitvi14g04489.
DR GeneID; 100257867; -.
DR Gramene; Vitvi00g04467_t001; Vitvi00g04467_P001; Vitvi00g04467.
DR Gramene; Vitvi14g04489_t001; Vitvi14g04489_P001; Vitvi14g04489.
DR KEGG; vvi:100257867; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; F6HB91; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000009183; Chromosome 13.
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; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
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:SF89; LIPOXYGENASE 2, CHLOROPLASTIC; 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 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:UP000009183}.
FT DOMAIN 89..209
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 212..903
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 259..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 102253 MW; 1F61734EE3BB64B9 CRC64;
MMMNASHYQL HRLNPTQSSS SLLHKPFILS HGRSISSPAY LPSRTTLNFH GKKKCFCIRA
SATDVRGVET SKENAASVKA VVRAAAAGLL SDLGITKPLD VYADLVGKTL LLELVSAEVD
SGTGLEKGTI KGYAHKVRHE KEEVVYESEF IVPAGFGEIG AILVENEHHK EMFINNIVLD
GLHNGPIHIN CSSWVHSKFD NPKKRIFFTN KSYLPDETPS GLTKLREMEL ENLRGNGKGE
RKTSDRIYDY DTYNDLGDPD DSEDLARPII GGKDHPYPRR CRTGRPSSKK DPLSEKRTSS
VYVPRDEAFE EVKQMTFSTK TLKSVLHALL PQVEIMLLDP HLGFPYFTAI DSLFQEGVPL
PKSKNFFQSI IPRLVKTIAE REGDILLFET PAMIDRDKFA WFRDEEFSRQ ALAGLNPYSL
QLVTEWPLKS ELDPEIYGPP ESLITAELIE KEIKGVMTID EALKQKKLFI LDYHDLLLPY
VNKVREIEGT TLYGSRTLFF LTMEGTLRPL AIELTRPPVG DKPQWKQVFT PGWDATSCWL
WRLAKTHVCA HDSGYHQLVV HWLRTHCCTE PYIIAANRQL SAMHPIYRLL HPHLRYTMEI
NALARESLIN AGGIIESCFS PGKYAIELSS AAYDQLWRFD MEALPADLIR RGMAVEDPTA
EHGLKLTIED YPFANDGLVL WDAIKQWVRD YVNHYYPDPS LVESDKELQG WWTEVRTKGH
ADKKDEPWWP VMKTPEDLIH VLTTIIWVTA GHHAAVNFGQ YVYAGYFPNR PTIARTNMPT
EDPSDEEFKN FLHKPEIALL KCFPSQIQAT KIMAVLDVLS SHSPDEEYLG DQMEPSWTEN
PIIKAAFERF NGRLKELEGI IDGRNTNLNL KNRTGAGVVP YELLKPFSKP GVTGMGVPNS
ISI
//
