LOX1_HORVU
ID LOX1_HORVU Reviewed; 862 AA.
AC P29114; Q42845; Q84QC4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Linoleate 9S-lipoxygenase 1;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase 1;
GN Name=LOX1.1; Synonyms=LOXA;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Triumph;
RX PubMed=7827128; DOI=10.1016/0005-2760(94)00231-m;
RA van Mechelen J.R., Smits M., Douma A.C., Rouster J., Cameron-Mills V.,
RA Heidekamp F., Valk B.E.;
RT "Primary structure of a lipoxygenase from barley grain as deduced from its
RT cDNA sequence.";
RL Biochim. Biophys. Acta 1254:221-225(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 512-862.
RX PubMed=14558691; DOI=10.1094/mpmi.2003.16.10.893;
RA Steiner-Lange S., Fischer A., Boettcher A., Rouhara I., Liedgens H.,
RA Schmelzer E., Knogge W.;
RT "Differential defense reactions in leaf tissues of barley in response to
RT infection by Rhynchosporium secalis and to treatment with a fungal
RT avirulence gene product.";
RL Mol. Plant Microbe Interact. 16:893-902(2003).
RN [3]
RP PROTEIN SEQUENCE OF 274-294 AND 832-845.
RC STRAIN=cv. Triumph; TISSUE=Embryo;
RX PubMed=1554746; DOI=10.1016/0167-4838(92)90429-h;
RA Doderer A., Kokkelink I., van der Veen S., Valk B.E., Schram A.W.,
RA Douma A.C.;
RT "Purification and characterization of two lipoxygenase isoenzymes from
RT germinating barley.";
RL Biochim. Biophys. Acta 1120:97-104(1992).
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. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer.
CC -!- DEVELOPMENTAL STAGE: In both quiescent and germinating seeds.
CC -!- MISCELLANEOUS: With linoleate as substrate, lipoxygenase 1 shows a
CC specificity for carbon 9 as the site for hydroperoxidation (in contrast
CC to lipoxygenase 2, which shows a preference for carbon 13).
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP04432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L35931; AAA64893.1; -; Genomic_DNA.
DR EMBL; AY220737; AAP04432.1; ALT_INIT; mRNA.
DR PIR; S21772; S21772.
DR PIR; S22236; S22236.
DR PIR; T05941; T05941.
DR AlphaFoldDB; P29114; -.
DR SMR; P29114; -.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0280010.1; HORVU.MOREX.r2.4HG0280010.1; HORVU.MOREX.r2.4HG0280010.
DR Gramene; HORVU.MOREX.r2.4HG0280010.1; HORVU.MOREX.r2.4HG0280010.1; HORVU.MOREX.r2.4HG0280010.
DR BRENDA; 1.13.11.58; 2687.
DR UniPathway; UPA00382; -.
DR ExpressionAtlas; P29114; baseline and differential.
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 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis.
FT CHAIN 1..862
FT /note="Linoleate 9S-lipoxygenase 1"
FT /id="PRO_0000220723"
FT DOMAIN 34..161
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 164..862
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 212..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
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 708
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 712
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 862
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 862 AA; 96393 MW; F55954473467BEAA CRC64;
MLLGGLIDTL TGANKSARLK GTVVLMRKNV LDLNDFGATI IDGIGEFLGK GVTCQLISST
AVDQDNGGRG KVGAEAELEQ WVTSLPSLTT GESKFGLTFD WEVEKLGVPG AIVVNNYHSS
EFLLKTITLH DVPGRSGNLT FVANSWIYPA ANYRYSRVFF ANDTYLPSQM PAALKPYRDD
ELRNLRGDDQ QGPYQEHDRI YRYDVYNDLG EGRPILGGNS DHPYPRRGRT ERKPNASDPS
LESRLSLLEQ IYVPRDEKFG HLKTSDFLGY SIKAITQGIL PAVRTYVDTT PGEFDSFQDI
INLYEGGIKL PKVAALEELR KQFPLQLIKD LLPVGGDSLL KLPVPHIIQE NKQAWRTDEE
FAREVLAGVN PVMITRLTEF PPKSSLDPSK FGDHTSTITA EHIEKNLEGL TVQQALESNR
LYILDHHDRF MPFLIDVNNL PGNFIYATRT LFFLRGDGRL TPLAIELSEP IIQGGLTTAK
SKVYTPVPSG SVEGWVWELA KAYVAVNDSG WHQLVSHWLN THAVMEPFVI STNRHLSVTH
PVHKLLSPHY RDTMTINALA RQTLINAGGI FEMTVFPGKF ALGMSAVVYK DWKFTEQGLP
DDLIKRGMAV EDPSSPYKVR LLVSDYPYAA DGLAIWHAIE QYVSEYLAIY YPNDGVLQGD
TEVQAWWKET REVGHGDLKD APWWPKMQSV PELAKACTTI IWIGSALHAA VNFGQYPYAG
FLPNRPTVSR RRMPEPGTEE YAELERDPER AFIHTITSQI QTIIGVSLLE VLSKHSSDEL
YLGQRDTPEW TSDPKALEVF KRFSDRLVEI ESKVVGMNHD PELKNRNGPA KFPYMLLYPN
TSDHKGAAAG LTAKGIPNSI SI
