ID A0A498K8W6_MALDO Unreviewed; 942 AA.
AC A0A498K8W6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=DVH24_038142 {ECO:0000313|EMBL:RXI03868.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI03868.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI03868.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI03868.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) 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 -!- 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:RU003975}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXI03868.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RDQH01000329; RXI03868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498K8W6; -.
DR STRING; 3750.A0A498K8W6; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000290289; Chromosome 3.
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; 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; 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};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU003975};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW ECO:0000256|RuleBase:RU003975};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT DOMAIN 113..244
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 247..942
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 48..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 106677 MW; FB6F78C08A650505 CRC64;
MLNPQVHQSK SAQTLFLHKP FIHGSAGSSF PVWSRPSFLP EKYRSIKATS SSSSSSDNSN
TPTTTTKTTT TTTRITTTAI PNPITPTPPP TTTTTTTIVT TEVVTKKFIS VKATLTVTLT
VGGFLSNLGL NRGLDDITDL LGQSLLLELV SAELHPETGE EKEKVAGYAH RSRRQEGEII
YETDIKVPVD FGEIGAILVE NEHHKEMFLK EIVVDGLPCG SVHHSCNSWI HSKYDNPEKR
VFFTNKSYLP SQTPSGLVRL REEELLTLRG NGQGERKSFE RIYDYDVYND LGDPDKNLRL
QRPVLGGKEF PHPRRCRTGR PPCDTDPLSE KRSRKHWYVP RDEAFSEVKQ LTFSAKTLYS
VMHALVPSLE MAIADTNLGF KYFTAIDSLF HEGIHLPPFK EQGVLKALLP RLVNVMATGD
DVLRFVPPET MNRDKFFWFR DEEFGRQTLA GLNPYSIKLV TEWPLKSELD PAIYGPPESA
ITNEIIEREI GGFATITEAI REKKLFILDY HDLFLPYVSK VRKLEGTTLY GSRTLFFLTP
EGTLRPLVIE LTRPPMDGKP QWKQVFQPAW NSTDVWLWRL AKAHVLAHDS GYHQLGIDYC
RLRTHCATEP YIIATNRQLS VMHPIYRLLH PHFRYTMEIN SLARDSLINA DGIIETSFSP
GKYSLELCSI AYGKEWRFDQ EALPADLIRR GMAVEDPTAP HGLRLTIEDY PFANDGLLLW
DAIKQWVTDY VNHYYPDSIL VQTDEELQAW WTEIKTVGHA DKKDEPWWPE LNTPEDLMGI
ITTMVWVASG HHAAVNFGQY AYGGYFPNRP TVARTNVPTE DPSEEDWKNF IKKPESALLQ
CFPSQIQATR IMAVLDILSN HSPDEEYIGE KMEQAWAEEP VIKAAFERFK GRLLALEGSI
DDRNANSELK NRHGAGVLPY ELLKPFSQPG VTGKGVPYSI SI
//
