ID A0A1Q3DAR6_CEPFO Unreviewed; 912 AA.
AC A0A1Q3DAR6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=CFOL_v3_32988 {ECO:0000313|EMBL:GAV89574.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV89574.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) 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}.
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:GAV89574.1}.
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DR EMBL; BDDD01005596; GAV89574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3DAR6; -.
DR STRING; 3775.A0A1Q3DAR6; -.
DR InParanoid; A0A1Q3DAR6; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000187406; 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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF95; LIPOXYGENASE 4, 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 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:UP000187406}.
FT DOMAIN 96..218
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 221..912
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 912 AA; 103336 MW; 98098033164EC9B5 CRC64;
MALAKEIMGS SMIERSSFVS SNNVFLSHRH QQMQSQLLVK PVLVPLQQSR VHLRRVGRGP
VAAISEDLFK TTVPDEVVNF KVRAVVTIRK KNKEDLKETL VKHLDAFTDK IGRNVVLELI
SNDVDPKTKA PKKSKEAVLK DWSKKANIRA ERVNYNAEFQ VDSKFGVPGA ITVTNKHQNE
FYLESITIEG FACGPVHFAC NSWVQSQKDH RGKRIFFSNK PYLPSETPAG LRALREKELK
DLSGNGKGVR KLSDRIYDFD VYNDLGNPDK ATTFARPSLG GENIPYPRRC RTGRLPSDTD
MHAESRVEKP LPMYVPRDEQ FEESKLDTFS AGRLKAVLHN LIPSLKASIS ADNFNAFSDI
DSLYKEGLLL KMGLQDELLK KFPKIVTKIQ ESSEGLLRYD TPKILSKDKF AWLRDDEFAR
QAVAGINPVN IERLEVYPPV SKLDHDTYGP PESALKEEHI IGHLNGMTVQ QALEQNKLYI
VDYHDVYLPF LDRINQLDGR KAYATRTIYF LTPNGTLKPI AIELSLPYTG PSSRSKRVVT
PPVDATSNWI WQLAKAHVCS NDAGVHQLVN HWLRTHACLE PFILAAHRQL SAMHPIFKLL
DPHMRYTLEI NALARQSLIN ADGVIESCFT PGRYCMEISA AAYKNHWRFD LETLPADLIR
RGMAVPDPTQ PHGLKLLFED YPYASDGLLI WSAIENWVRT YVHHYFPNSS LICNDEELQA
WYAESINVGH ADLRHADWWP TLETVDDLVS ILTTIIWLAS AQHAALNFGQ YSYGGYVPNR
PPLMRRLIPQ ENDLEYANFL ADPQKYFLNA IPSLLQATKF MAVVDTLSTH SPDEEYLGER
QQPSIWTGDA EIVEAFYEFS AKIRRIEKEI ERRNGDPSLR HRCGAGVIPY ELLVPSSEPG
VTCRGVPNSV SI
//
