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Database: UniProt
Entry: D8SN12_SELML
LinkDB: D8SN12_SELML
Original site: D8SN12_SELML 
ID   D8SN12_SELML            Unreviewed;       852 AA.
AC   D8SN12;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Lipoxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SELMODRAFT_234610 {ECO:0000313|EMBL:EFJ14272.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ14272.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|RuleBase:RU003974};
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; GL377628; EFJ14272.1; -; Genomic_DNA.
DR   RefSeq; XP_002984627.1; XM_002984581.1.
DR   AlphaFoldDB; D8SN12; -.
DR   STRING; 88036.D8SN12; -.
DR   EnsemblPlants; EFJ14272; EFJ14272; SELMODRAFT_234610.
DR   GeneID; 9644758; -.
DR   Gramene; EFJ14272; EFJ14272; SELMODRAFT_234610.
DR   KEGG; smo:SELMODRAFT_234610; -.
DR   eggNOG; ENOG502QVKD; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   InParanoid; D8SN12; -.
DR   OMA; RESEWMT; -.
DR   OrthoDB; 462210at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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-KW.
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; IPR020833; LipOase_Fe_BS.
DR   InterPro; IPR001246; LipOase_plant.
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:SF91; 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; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
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   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   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   DOMAIN          36..163
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          166..852
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
SQ   SEQUENCE   852 AA;  94832 MW;  FBC54CA85B862FA6 CRC64;
     MPRVLRLAGS LLGNNTPSDQ IVYKGIVVVQ KPSSLCVTDV GASMVANAAN FLGMGITLQL
     ISSTAIDSST NTGKLSKPAA LEKWLLSPVV LFGTDEVKYS VKFTVDPDFG LPGAFSINNG
     HLNEFFLVSL TVELPGGGKH VEFPCHSWVF NSRAYKTKRI FFSNEFYLPA DTPKGLITAR
     YNDLIALRGN GSGTRKACDR IYDYDVYNDL GNPLLNAAKR PVMGGSKEYP YPRRCRTGRT
     IFIGVETSGL NLLADYYIPS DERFSSVKAT SFLADGLKSL THGVLPILKT VTGFKQTFGS
     FKEVKDLYDQ GLDLSKIVTA PINGIKTPFQ LFNQLNADTG NTSFMKFPVP QVFKADEKGW
     MLDSEFAREM LSGLNPMVIE ALTEFPPMST LDSAKYGPQK SAITEKHIVN LLEGLTVQKA
     LDKKKLFIVN YHDSYMPYLD KINSRQKIYA YASRTLLYLK SDGTLQPVAI ELNTPYSQRV
     FVPPAAGQID WLWELAKAHA AANDAGYHQL VSHWLRTHAC VEPFIIATNR QLSKLHPLNT
     FLQPHFKNTM AINAKARKSL INAKGIIERT FSLRRYSVEM SSLAYKGWRF DQEGLPADLL
     KRGMAVPDAT SKGGVKLIVE DYPYAVDGLE IWTAIEKWVT DYLEIYYKND ASVTSDPELQ
     AWWSELINKG HADKKDEKWW IKLDSKKSLT SVLTTLIWIA SAHHAAVNFG QYAYAGYMPN
     RPTTTHRPIP EKDSDEHKKL LADPERFFLS CVSSKMEAIL CLLTVEILSS HAAEEEYLGQ
     RAVENWTANA NVKAAFVAFG EELRKVERSI INRNNDPALK NRVGAVNVPY TLLYPSSANG
     ITGKGIPNSI SI
//
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