ID A0A0L9UNU1_PHAAN Unreviewed; 857 AA.
AC A0A0L9UNU1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=HKW66_Vig0213660 {ECO:0000313|EMBL:KAG2371192.1},
GN LR48_Vigan05g201800 {ECO:0000313|EMBL:KOM44413.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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=3914 {ECO:0000313|EMBL:KOM44413.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM44413.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM44413.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2371192.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2371192.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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; JABFOF010000011; KAG2371192.1; -; Genomic_DNA.
DR EMBL; CM003375; KOM44413.1; -; Genomic_DNA.
DR RefSeq; XP_017422959.1; XM_017567470.1.
DR AlphaFoldDB; A0A0L9UNU1; -.
DR STRING; 3914.A0A0L9UNU1; -.
DR EnsemblPlants; KOM44413; KOM44413; LR48_Vigan05g201800.
DR GeneID; 108332293; -.
DR Gramene; KOM44413; KOM44413; LR48_Vigan05g201800.
DR KEGG; var:108332293; -.
DR OMA; CEWELAK; -.
DR OrthoDB; 888244at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000053144; Chromosome 5.
DR Proteomes; UP000743370; Unassembled WGS sequence.
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:SF122; LINOLEATE 9S-LIPOXYGENASE-4; 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 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:UP000053144}.
FT DOMAIN 37..163
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 166..857
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 219..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 96530 MW; 604EF8774FA8AF46 CRC64;
MSLLGGIFGN KQKIKGTVVL MRKNVLDINT ILNPANVVDS VLDLAGSLVD AVTAFATSIS
IQLISSTKAD GQGKGKVGTA TKLRGQISLP TLGASEEAYD VNFEWDSDFG IPGAFYIKNF
MQNEFYLKSL TLEDIPNHGT IHFVCNSWVY NSKVYKTDRI FFANNTYLPG ETPAPLVKYR
EEELKVVRGD GTGERKEWDR VYDYDVYNDL GNPDKGEALA RPVLGGSTLP YPRRGRTGRP
KTTKDPNSEK PSDFVYLPRD EAFGHLKSSD FLAYALKSVS QDVLPVLTDA FDGNILSLEF
DSFAEVHKLY EGGVTLPTDF LSKYAPIPIV KELFRSDGEQ FLKYPPPKVM QVDKSAWMTD
EEFARETIAG VNPNVIKILK EFPPRSTLDT QAFGDHTSII TKEHLEPQLG GLTVEQAIEN
NKLFILDHHD YLIPYLRKIN SSTTKTYATR TIFFLKEDGT LTPLAIELSK PHDQGEEYGP
ISEVYVPAYE GVEAYIWLLA KAYVIVNDSC YHQIVSHWLS THAVVEPFVI ATNRQLSVVH
PVYKLLFPHY RDTMNINSLA RKSLVNADGI IEKTFLWSRY SMEMSAVIYK DWSFVDQALP
NDLVKRGVAV KDPSAPHGVK LLIEDYPYAS DGLEIWAAIK SWVEEYVAFY YKSDEALQKD
PELQAWWKEL VQVGHGDLKD KPWWPKMQTR GELVDVSTTL IWISSALHAA VNFGQYPYGG
LILNRPTISR RFMPEKGSAE YDALAKNPEK EFLRTITGKK ETLIDLTVIE ILSRHASDEF
YLGEREGGDF WTSDAGPLEA FKRFGTKLAE IEQKLVQKNN DETLRNRTGP AKMPYTLLFP
SSEEGLTFRG IPNSISI
//
