LOX3_PEA
ID LOX3_PEA Reviewed; 861 AA.
AC P09918;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Seed linoleate 9S-lipoxygenase-3;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase-3;
GN Name=LOX1.3;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Birte;
RX PubMed=3140791; DOI=10.1042/bj2530915;
RA Ealing P.M., Casey R.;
RT "The complete amino acid sequence of a pea (Pisum sativum) seed
RT lipoxygenase predicted from a near full-length cDNA.";
RL Biochem. J. 253:915-918(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Birte;
RA Casey R.;
RL Submitted (APR-1994) 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. It catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X07807; CAA30666.1; -; mRNA.
DR EMBL; X78581; CAA55319.1; -; Genomic_DNA.
DR PIR; S01142; S01142.
DR AlphaFoldDB; P09918; -.
DR SMR; P09918; -.
DR BRENDA; 1.13.11.B6; 4872.
DR UniPathway; UPA00382; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 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; PTHR11771; 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; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 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 Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis.
FT CHAIN 1..861
FT /note="Seed linoleate 9S-lipoxygenase-3"
FT /id="PRO_0000220714"
FT DOMAIN 41..166
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 169..861
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 215..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 522
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 527
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 713
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 717
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 861
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 861 AA; 97629 MW; 442510278225D750 CRC64;
MFSGVTGILN RGHKIKGTVV LMRKNVLDIN SLTTVGGVIG QGFDILGSTV DNLTAFLGRS
VSLQLISATK PDATGKGKLG KATFLEGIIS SLPTLGAGQS AFKIHFEWDD DMGIPGAFYI
KNFMQTEFFL VSLTLDDIPN HGSIYFVCNS WIYNAKHHKI DRIFFANQTY LPSETPAPLV
HYREEELNNL RGDGTGERKE WERIYDYDVY NDLGNPDSGE NHARPVLGGS ETYPYPRRGR
TGRKPTRKDP NSESRSDYVY LPRDEAFGHL KSSDFLTYGL KAVSQNVVPA LESVFFDLNF
TPNEFDSFDE VHGLYEGGIK LPTNILSQIS PLPVLKEIFR TDGENTLKYP PPKVIQVSRS
GWMTDEEFAR EMLAGVNPNV ICCLQEFPPR SKLDSQIYGD HTSKISKEHL EPNLEGLTVE
EAIQNKKLFL LDHHDSIMPY LRRINSTSTK AYATRTILFL NNNQNLKPLA IELSLPHPQG
DEHGAVSYVY QPALEGVESS IWLLAKAYVI VNDSCYHQLV SHWLNTHAVV EPFVIATNRH
LSCLHPIYKL LYPHYRDTMN INSLARLSLV NDGGIIEKTF LWGRYSMEMS SKVYKNWVFT
EQALPADLIK RGMAIEDPSS PCGVKLVVED YPYAVDGLEI WAIIKTWVQD YVSLYYTSDE
KLRQDSELQA WWKELVEVGH GDKKNEPWWP KMQTREDLIE VCSIVIWTAS ALHAAVNFGQ
YSYGGLILNR PTLSRRFMPE KGSAEFEELV KSPQKAYLKT ITPKFQTLID LSVIEILSRH
ASDELYLGER DNPNWTSDKR ALEAFKKFGN KLAEIEKKLT QRNNDEKLRN RHGPVEMPYT
LLYPSSKEGL TFRGIPNSIS I
