ID K7QK66_CAPAN Unreviewed; 859 AA.
AC K7QK66;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=DAD1 {ECO:0000313|EMBL:AFU51542.1};
GN ORFNames=T459_03559 {ECO:0000313|EMBL:PHT95677.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:AFU51542.1};
RN [1] {ECO:0000313|EMBL:AFU51542.1}
RP NUCLEOTIDE SEQUENCE.
RA Gong Z., Jia Q., Li D.;
RT "Specific expression genes from Capsicum annuum after inoculated with
RT Phytophthora capsici.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHT95677.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441736; DOI=10.1038/ng.2877;
RA Kim S., Park M., Yeom S.I., Kim Y.M., Lee J.M., Lee H.A., Seo E., Choi J.,
RA Cheong K., Kim K.T., Jung K., Lee G.W., Oh S.K., Bae C., Kim S.B.,
RA Lee H.Y., Kim S.Y., Kim M.S., Kang B.C., Jo Y.D., Yang H.B., Jeong H.J.,
RA Kang W.H., Kwon J.K., Shin C., Lim J.Y., Park J.H., Huh J.H., Kim J.S.,
RA Kim B.D., Cohen O., Paran I., Suh M.C., Lee S.B., Kim Y.K., Shin Y.,
RA Noh S.J., Park J., Seo Y.S., Kwon S.Y., Kim H.A., Park J.M., Kim H.J.,
RA Choi S.B., Bosland P.W., Reeves G., Jo S.H., Lee B.W., Cho H.T., Choi H.S.,
RA Lee M.S., Yu Y., Do Choi Y., Park B.S., van Deynze A., Ashrafi H., Hill T.,
RA Kim W.T., Pai H.S., Ahn H.K., Yeam I., Giovannoni J.J., Rose J.K.,
RA Sorensen I., Lee S.J., Kim R.W., Choi I.Y., Choi B.S., Lim J.S., Lee Y.H.,
RA Choi D.;
RT "Genome sequence of the hot pepper provides insights into the evolution of
RT pungency in Capsicum species.";
RL Nat. Genet. 46:270-278(2014).
RN [3] {ECO:0000313|EMBL:PHT95677.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC Evidence={ECO:0000256|ARBA:ARBA00036508};
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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; JQ219047; AFU51542.1; -; mRNA.
DR EMBL; AYRZ02000001; PHT95677.1; -; Genomic_DNA.
DR RefSeq; NP_001311581.1; NM_001324652.1.
DR AlphaFoldDB; K7QK66; -.
DR STRING; 4072.K7QK66; -.
DR EnsemblPlants; PHT95677; PHT95677; T459_03559.
DR GeneID; 107847934; -.
DR Gramene; PHT95677; PHT95677; T459_03559.
DR KEGG; cann:107847934; -.
DR OMA; ENWLTTI; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000222542; Chromosome 1.
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:SF178; LINOLEATE 9S-LIPOXYGENASE A; 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 2: Evidence at transcript level;
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:UP000222542}.
FT DOMAIN 28..158
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 161..859
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 208..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 97041 MW; 0F6B217E9C3D718B CRC64;
MIKNLVDGLI HHDSSKKVKG TVVMMKKNAL DFTDLAGSLT DKLFEALGQK VSLQLISSVQ
GDPANGLQGK HSNPAYLENF LFTPTRLTAG ESAFGVTFDW NEEFGVPGAF TIKNSHINEF
FLKSLILEDV PNHGKVHFVC NSWVYPSFRY KTDRIFFANQ PYLPSETPEP LRKYRESELK
TLRGDGTGKL EAWNRVYDYD VYNDLGNPDQ GPEHVRTTLG GSADYPYPRR GRTSRPPTRT
DPKSESRIPL LLSLDIYVPR DERFGHLKLS DFLTYALKSL VQFILPELHA LFDGTPNEFD
SFEDVLRLYE GGIKLPQGPL FKALTDAIPL EMIRELLRTD GEGILRFPTP LVIKDSKSAW
RTDEEFAREM LAGVNPVIIS RLQEFPPKSK LDPNVYGNQD STITAEHIQD KLDGLTIDQA
INNNKLFILN HHDILTPYLR RINTTTTKTY ASRTLLFLQD NGSLKPLAIE LSLPHPDGDQ
FGVISKVYTP SDQGVESSIW QLAKAYAAVN DSGVHQLISH WLNTHAVIEP FVIATNRQLS
VLHPIHKLLY PHFRDTMNIN ALARQILINA GGVLESTVFP SKYAMEMSAV VYKDWVFPDQ
ALPADLIKRG IAVEDSSSPH GVRLLIQDYP YAVDGLEIWS AIKSWVTEYC NVYYKSNEDI
LKDNELQEWW KELREVGHGD KKDAPWWPEM ESPEDLIESC TIIIWIASAL HAAVNFGQYP
YAGYLPNRPT VSRRFMPEPG TPEYEELKTN PDKAFLKTIT AQFQTLLGVS LIEILSRHTS
DEIYLGQRES PEWTKDKEPL AAFDRFGKKL TEIENHIIQR NGDQILKNRS GPVNAPYTLL
FPTSEGGLTG KGIPNSVSI
//