LOXB_PHAVU
ID LOXB_PHAVU Reviewed; 741 AA.
AC P27481;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Linoleate 9S-lipoxygenase;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase;
DE EC=1.13.11.12;
DE Flags: Fragment;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Red Mexican; TISSUE=Leaf;
RX PubMed=8400375; DOI=10.1094/mpmi-6-453;
RA Slusarenko A.J., Meier B.M., Shaw N.;
RT "Spatial and temporal accumulation of defense gene transcripts in bean
RT (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive
RT cell death.";
RL Mol. Plant Microbe Interact. 6:453-466(1993).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC EC=1.13.11.12;
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X63521; CAA45086.1; -; mRNA.
DR PIR; S18906; S18906.
DR AlphaFoldDB; P27481; -.
DR SMR; P27481; -.
DR STRING; 3885.XP_007150489.1; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR UniPathway; UPA00382; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:UniProtKB-EC.
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 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; 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..>741
FT /note="Linoleate 9S-lipoxygenase"
FT /id="PRO_0000220716"
FT DOMAIN <1..53
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 56..741
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 108..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 412
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 598
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 602
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT NON_TER 1
FT NON_TER 741
SQ SEQUENCE 741 AA; 84197 MW; 2F2CDD5979606AC1 CRC64;
IPGAFYIKNF MQVEFYLKSL TLEDIPNHGT IHFICNSWIY NSKVYKSDRI FFANNTYLPS
ETPAPLLKYR EEELKNVRGD GSGERKEWDR VYDYDVYNDL GNPDKGAALA RPVLGGSTLP
YPRRGRTGRP KTKKDPNSEK PSDFVYLPRD EAFGHLKSSD FLAYGLKSVS QDVLPVLTDA
FDGNLLSLEF DNFAEVHKLY EGGVTLPTNF LSKYAPIPIV KEIFRSDGEQ FLKYPPPKVM
QVNKSAWMTD EEFARETIAG VNPNVIKSLE EFPPRSKLDT QSFGDHTSII TKEHLEINLG
GLTVEQAIQS KKLFILDHHD YLIPYLRRIN ASATKTYATR TIFFLKSDGT LAPLAIELSK
PHPQGDEHGP VSEVYVPAYE GVEAYIWLLA KAYVVVNDSC YHQLVSHWLN THAVVEPFVL
ATNRQLSVVH PVYKLLFPHY RDTMNINSLA RKSLVNADGI IEKTFLWGRY ALELSAVIYK
DWSLHDQALP NDLVKRGVAV KDPSAPHGVK LVIEDYPYAS DGLEIWDAIK SWVVEYVAFY
YKSDEVLQQD SELQAWWKEL VQVGHGDLKD KPWWPKMQSR ENLVEVSTTL IWIASALHAA
VNFGQYPYGG LILNRPTISR RFMPEKGSAE YAALAKNPEK EFLKTITGKK ETLIDLTVIE
ILSRHASDEI YLGERDGGDH WTSDAGPLEA FKRFGKKLAE IEKKLVQKNN DETLRNRTGP
AKMPYTLLYP SSEEGLTFRG I
