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Database: UniProt
Entry: A0A061DM32_THECC
LinkDB: A0A061DM32_THECC
Original site: A0A061DM32_THECC 
ID   A0A061DM32_THECC        Unreviewed;       443 AA.
AC   A0A061DM32;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   22-FEB-2023, entry version 44.
DE   RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN   ORFNames=TCM_002658 {ECO:0000313|EMBL:EOX93735.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX93735.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX93735.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|RuleBase:RU003974}.
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DR   EMBL; CM001879; EOX93735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DM32; -.
DR   EnsemblPlants; EOX93735; EOX93735; TCM_002658.
DR   Gramene; EOX93735; EOX93735; TCM_002658.
DR   HOGENOM; CLU_004282_1_0_1; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000026915; 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; 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   Gene3D; 3.10.450.60; -; 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   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF91; LIPOXYGENASE; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00468; PLTLPOXGNASE.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU003975};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU003975};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU003975};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU003975};
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|RuleBase:RU003975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT   DOMAIN          1..443
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
SQ   SEQUENCE   443 AA;  51355 MW;  C744AA03888ABFAE CRC64;
     MNQWRIFILD HHDYVLPFLG KINSEGVCAY ASRALLFLRE DATLKPLAIE LSYPVSSDSN
     EMESRVFLPA KEGTDRALWQ LAKAHVAAND SAYHQLISHW LHTHAVVEPF IIATRRQLSV
     MHPVHRLLEP HFKDTMHINA LARSILINSG GILEKTLFTG KFSMELSSEL YKEWRFDEQA
     LPSDLVKRRM ALEDPESPTE AQILFQDYPY GLDGLDVWLA IDTWVKDFCD LFYEDDDSVK
     SDTEIQGWWS EIRNVGHGDK RNETWWYQMT TKTDLTKTLT TLIWISSALH ASVNFGQYAY
     AGYPPNRPTR CRKFIPDEGT MEFAEFLEDP DKYFLNMLPE RFEATLGIAL MEVLSRHTSD
     EVYLGQRPTS EWIDNNEVKQ KFEKFIESLQ EIEKQVMERN RDSKLKNRCG PIKMPYRLLY
     PDATKVEFRE GITAKGIPNS VSI
//
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