ID A0A1S2YMN1_CICAR Unreviewed; 907 AA.
AC A0A1S2YMN1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=LOC101499921 {ECO:0000313|RefSeq:XP_004507121.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004507121.1};
RN [1] {ECO:0000313|RefSeq:XP_004507121.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004507121.1};
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_004507121.1; XM_004507064.3.
DR AlphaFoldDB; A0A1S2YMN1; -.
DR STRING; 3827.A0A1S2YMN1; -.
DR PaxDb; 3827-XP_004507121-1; -.
DR GeneID; 101499921; -.
DR KEGG; cam:101499921; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000087171; Chromosome Ca6.
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:SF194; LINOLEATE 13S-LIPOXYGENASE 2-1, CHLOROPLASTIC; 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:UP000087171}.
FT DOMAIN 88..208
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 211..907
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 907 AA; 103993 MW; D14844924CE8C574 CRC64;
MLMQQINVSN IRPNCLILHK PCLQGTGHII NSHPCFEFPY QKKQRRYRNR NGCSIKTVTE
AKNEVIEIEK NSTKVKATVS VIPTVVGILS ELGIERGLDD IKDLIGQSIF LELLSAQLDP
ETALEKVSIK GYVHLTHRSI EEIKYEGEFE VPGSFGEIGA ILVENEHHRE MFMRGIVVDG
FLTGPVNFTC ESWVHSKYDN PDKRVFFSNK SYLPSETPEG LKRLREEELI ILRGNGEGER
KKFERIYDYD VYNDLGNPDT DPELKRHVLG GTQHPYPRRC RTGRPRCQTD PLSEKRSNSV
YVPRDECFSE VKQVTFSTNT LHSGLHALLP ALRTAIIDTN LGFPLFSSID DLFNQGFNLP
PSKDKGFLNL RTVLPRLVKC VQDTRNDFLR FETPATMDKD RFFWFRDEEF GRQTIAGLNP
CCIQLVTEWP LKSKLDPNIY GPAESAITTE IIEREISGFT TVEKAIKEKK LFILDYHDFF
LPLVEEVRKL EGTTLYGSRT LFFLTHDGTL RPLAIELTRP PMDGKPQWRQ VFTPSWHSTA
VWLWRLAKAH VLAHDSSYHQ LVSHWLRTHC CTEPYIIATN RQLSAMHPIY RLLLPHFRYT
MEINVLAREA LINADGIIES SFTPKKLSIL VSSMAYDQHW QFDLQALPND LIHRGMAEKD
PNAPHGLKLA IEDYPYANDG LLLWDAIKSW VTDYVKHYYK ESSFVVEKDE ELQAWWEEIK
NVGHGDKKDE TWWPNLKTNE DLIEILTTIV WITSGHHAAV NFGQYNYAGY FPNRPAIARN
NMPTEDPLDQ EWELFLEKPE VTLLNCFPSQ IQATTVMTVL DILSSHSPDE EYLGQTIEPA
WEEDPMVKAA FLKFKGKLLE LEGVIDERNA DSTRNNRNGA GILPYELLKP TSEPGVTGKG
VPYSISI
//
