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P27481

- LOXB_PHAVU

UniProt

P27481 - LOXB_PHAVU

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Protein
Linoleate 9S-lipoxygenase
Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.

Catalytic activityi

Linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.
Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.
Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.

Cofactori

Binds 1 iron ion per subunit. Iron is tightly bound By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi407 – 4071Iron; catalytic By similarity
Metal bindingi412 – 4121Iron; catalytic By similarity
Metal bindingi598 – 5981Iron; catalytic By similarity
Metal bindingi602 – 6021Iron; catalytic By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. linoleate 13S-lipoxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. oxylipin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Linoleate 9S-lipoxygenase (EC:1.13.11.58)
Alternative name(s):
Lipoxygenase (EC:1.13.11.12)
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›741›741Linoleate 9S-lipoxygenase
PRO_0000220716Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP27481.
SMRiP27481. Positions 1-741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini‹1 – 53›53PLAT
Add
BLAST
Domaini56 – 741686Lipoxygenase
Add
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P27481-1 [UniParc]FASTAAdd to Basket

« Hide

IPGAFYIKNF MQVEFYLKSL TLEDIPNHGT IHFICNSWIY NSKVYKSDRI    50
FFANNTYLPS ETPAPLLKYR EEELKNVRGD GSGERKEWDR VYDYDVYNDL 100
GNPDKGAALA RPVLGGSTLP YPRRGRTGRP KTKKDPNSEK PSDFVYLPRD 150
EAFGHLKSSD FLAYGLKSVS QDVLPVLTDA FDGNLLSLEF DNFAEVHKLY 200
EGGVTLPTNF LSKYAPIPIV KEIFRSDGEQ FLKYPPPKVM QVNKSAWMTD 250
EEFARETIAG VNPNVIKSLE EFPPRSKLDT QSFGDHTSII TKEHLEINLG 300
GLTVEQAIQS KKLFILDHHD YLIPYLRRIN ASATKTYATR TIFFLKSDGT 350
LAPLAIELSK PHPQGDEHGP VSEVYVPAYE GVEAYIWLLA KAYVVVNDSC 400
YHQLVSHWLN THAVVEPFVL ATNRQLSVVH PVYKLLFPHY RDTMNINSLA 450
RKSLVNADGI IEKTFLWGRY ALELSAVIYK DWSLHDQALP NDLVKRGVAV 500
KDPSAPHGVK LVIEDYPYAS DGLEIWDAIK SWVVEYVAFY YKSDEVLQQD 550
SELQAWWKEL VQVGHGDLKD KPWWPKMQSR ENLVEVSTTL IWIASALHAA 600
VNFGQYPYGG LILNRPTISR RFMPEKGSAE YAALAKNPEK EFLKTITGKK 650
ETLIDLTVIE ILSRHASDEI YLGERDGGDH WTSDAGPLEA FKRFGKKLAE 700
IEKKLVQKNN DETLRNRTGP AKMPYTLLYP SSEEGLTFRG I 741
Length:741
Mass (Da):84,197
Last modified:August 1, 1992 - v1
Checksum:i2F2CDD5979606AC1
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei741 – 7411

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X63521 mRNA. Translation: CAA45086.1.
PIRiS18906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X63521 mRNA. Translation: CAA45086.1 .
PIRi S18906.

3D structure databases

ProteinModelPortali P27481.
SMRi P27481. Positions 1-741.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00382 .

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProi IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Spatial and temporal accumulation of defense gene transcripts in bean (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive cell death."
    Slusarenko A.J., Meier B.M., Shaw N.
    Mol. Plant Microbe Interact. 6:453-466(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Red Mexican.
    Tissue: Leaf.

Entry informationi

Entry nameiLOXB_PHAVU
AccessioniPrimary (citable) accession number: P27481
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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