ID F6HZ11_VITVI Unreviewed; 869 AA.
AC F6HZ11;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN OrderedLocusNames=VIT_14s0128g00790 {ECO:0000313|EMBL:CCB59925.1};
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:CCB59925.1, 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; FN596501; CCB59925.1; -; Genomic_DNA.
DR AlphaFoldDB; F6HZ11; -.
DR STRING; 29760.F6HZ11; -.
DR PaxDb; 29760-VIT_14s0128g00790-t01; -.
DR EnsemblPlants; Vitvi14g00234_t004; Vitvi14g00234_P004; Vitvi14g00234.
DR Gramene; Vitvi14g00234_t004; Vitvi14g00234_P004; Vitvi14g00234.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; F6HZ11; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000009183; Chromosome 14.
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:SF126; LINOLEATE 9S-LIPOXYGENASE 1; 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 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 43..168
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 171..869
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 233..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 99297 MW; DB17EF640AD2738E CRC64;
MDMMMMMMKK KLLSIVSAIT GENDKKKIEG TIVLMKKNVL DFNDFNAPVR DRVHELFGQG
VSLQLVSAVH GDPANGLQGK IGKPAYLEDW IITITSLTAG ESAFKVTFDW DEEIGEPGAF
IIRNNHHSEF YLRTLTLEDV PGRGRIHFVC NSWVYPAQHY KTDRVFFTNQ TYLPSETPGP
LRKYREGELV NLRGDGTGKL KEWDRVYDYA YYNDLGNPDR DLKYARPVLG GSAEYPYPRR
GRTGRPPSEK DPNTESRLPL VMSLNMYVPR DERFGHLKMS DFLAYALKSI VQFLLPEFEA
LCDITHNEFD SFQDVLDLYE GGIKVPEGPL LDKIKDNIPL EMLKELVRTD GEHLFKFPMP
QVIKEDKSAW RTDEEFAREM LAGLNPVVIR LLQEFPPKSK LDPEIYGNQN SSITKEHIEN
HLDDLTINEA MEKKRLFILD HHDVFMQYLR RINTTSTKTY ASRTLLFLKD DGTLKPLAIE
LSLPHPSGDK FGAVNKVYTP AENGVEGSIW QLAKAYAAVN DSGYHQLLSH WLNTHAAIEP
FVIATNRQLS VLHPIHKLLH PHFRDTMNIN ALARQILINA GGVVESTVFP SKYAMEMSSV
VYKDWVLTEQ ALPADLIKRG MAVEDSEAPH GLRLLIDDYP YAVDGLEIWS AIETWVKEYC
SFYYKTDEMV QKDSELQSWW KEVREEGHGD KKDEPWWPKM HTVKELIETC TIIIWVASAL
HAAVNFGQYP YAGYLPNRPT ISRRFMPEEG TPEYEELKSN PDKAFLKTIT AQLQTLLGIS
LIEILSRHSS DEVYLGQRDT PEWTLDTTPL KAFEKFGRKL ADIEERIIDR NGNERFKNRV
GPVKIPYTLL YPTSEGGITG KGIPNSVSI
//
