UniProtKB - Q8RNT4 (LOX_PSEAI)
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>sp|Q8RNT4|LOX_PSEAI Linoleate 9/13-lipoxygenase OS=Pseudomonas aeruginosa OX=287 GN=lox PE=1 SV=2 MKRRSVLLSGVALSGTALANDSIFFSPLKYLGAEQQRSIDASRSLLDNLIPPSLPQYDNL AGKLARRAVLTSKKLVYVWTENFANVKGVPMARSVPLGELPNVDWLLKTAGVIVELIVNF VASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIA LLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVA GPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAV DKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMA KTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGA ARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPY RDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQL VEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTL VALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATI RTRNQARRKPYEYLLPSRIPASTNIHelp videoAdd a publicationFeedback
Protein
Linoleate 9/13-lipoxygenase
Gene
lox
Organism
Pseudomonas aeruginosa
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
In presence of oxygen, converts linoleate into (9S)-hydroperoxy-10,12-octadecenoate (9HPOD), which spontaneously decomposes to the corresponding 9-hydroxy-10,12-octadecenoate (9HOD), and into 13-hydroperoxy-9,11-octadecenoate (13HPOD) which spontaneously decomposes to the corresponding 13-hydroxy-9,11-octadecenoate (13HOD). Also active on linolenate. To a lesser extent, is also able to convert oleate into (10S)-hydroperoxy-8E-octadecenoate, which spontaneously decomposes to the corresponding 10-hydroxy-8E-octadecenoate. Is almost not active on arachidonate.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Miscellaneous
In vitro, under anaerobic conditions, does not transform linoleate or oleate into the corresponding hydroxy derivative.
Caution
The biochemical characterization done in PubMed:15028873 is devoted to oleic acid, however, the preferred substrate of the enzyme is linoleic acid.Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- (9Z,12Z)-octadecadienoateEC:1.13.11.58
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Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z,12Z)-octadecadienoate- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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=(9S)-hydroperoxy-(10E,12Z)-octadecadienoate- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoateEC:1.13.11.77
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Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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=(8E,10S)-10-hydroperoxy-octadeca-8-enoate- Search proteins in UniProtKB for this molecule.
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- (9Z,12Z)-octadecadienoateEC:1.13.11.77
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Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z,12Z)-octadecadienoate- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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=(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate- Search proteins in UniProtKB for this molecule.
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- (9Z,12Z,15Z)-octadecatrienoateEC:1.13.11.77
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Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa 42A2."
Vidal-Mas J., Busquets M., Manresa A.
Antonie Van Leeuwenhoek 87:245-251(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z,12Z,15Z)-octadecatrienoate- Search proteins in UniProtKB for this molecule.
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=(8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate- Search proteins in UniProtKB for this molecule.
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- (9Z,12Z)-octadecadienoateEC:1.13.11.12
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Manual assertion based on experiment ini
- Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z,12Z)-octadecadienoate- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate- Search proteins in UniProtKB for this molecule.
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- (9Z,12Z,15Z)-octadecatrienoateEC:1.13.11.12
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Manual assertion based on experiment ini
- Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z,12Z,15Z)-octadecatrienoate- Search proteins in UniProtKB for this molecule.
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=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Fe cation
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<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
Manual assertion inferred by curator fromi
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Inhibited by Ba2+, Zn2+ and Fe3+.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
kcat is 96 sec(-1) with linoleate as substrate (Ref. 4).
- KM=78.9 µM for linoleate (Ref. 4)2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.74 mM for oleate2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.66 mM for linoleate2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=0.73 mM for linolenate2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=0.246 µmol/min/mg enzyme with oleate as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=81.75 µmol/min/mg enzyme with linoleate as substrate (Ref. 4)2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
pH dependencei
Optimum pH is 7 with linoleate as substrate, and 8.5-9.0 with oleate as substrate.2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Temperature dependencei
Optimum temperature is 25-30 degrees Celsius. Active up to 45 degrees Celsius, less active after 50 degrees Celsius and completely inactive at 70 degrees Celsius.2 Publications
Manual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Cloning, expression and characterization of the lipoxygenase of Pseudomonas aeruginosa 42A2."
Vidal-Mas J.
Thesis (2005), University of Barcelona, SpainCited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 377 | Iron; catalyticPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| Metal bindingi | 382 | Iron; catalyticPROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
| Metal bindingi | 555 | Iron; catalyticPROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
| Metal bindingi | 559 | Iron; catalyticPROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
| Metal bindingi | 685 | Iron; via carboxylate; catalyticPROSITE-ProRule annotation Manual assertion according to rulesi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- linoleate 13S-lipoxygenase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Dioxygenase, Oxidoreductase |
| Ligand | Iron, Metal-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Linoleate 9/13-lipoxygenase (EC:1.13.11.12
Manual assertion based on experiment ini
Manual assertion based on experiment ini
Alternative name(s): Oleate 10S-lipoxygenase (EC:1.13.11.77
Manual assertion based on experiment ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:lox |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Pseudomonas aeruginosa |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 287 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Periplasm PROSITE-ProRule annotation
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
GO - Cellular componenti
- periplasmic space Source: UniProtKB-SubCell
Keywords - Cellular componenti
Periplasm<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 19 | Sequence analysisAdd BLAST | 19 | |
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000018330 | 20 – 685 | Linoleate 9/13-lipoxygenaseAdd BLAST | 666 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | Q8RNT4 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer.
1 PublicationManual assertion based on experiment ini
- Ref.3"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid."
Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A.
Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 287.DR97_765 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 23 – 25 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 26 – 28 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 33 – 47 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 55 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 60 – 76 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 79 – 81 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 91 – 94 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 97 – 99 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 103 – 122 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Helixi | 126 – 129 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 130 – 132 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 133 – 159 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 27 | |
| Helixi | 161 – 166 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 168 – 199 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 32 | |
| Helixi | 210 – 214 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 215 – 218 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 224 – 227 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 231 – 240 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 261 – 268 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 274 – 279 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 283 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 289 – 294 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 300 – 302 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 303 – 305 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 306 – 309 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 314 – 319 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 326 – 335 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Turni | 337 – 339 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 342 – 344 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 351 – 374 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| Helixi | 375 – 381 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 382 – 395 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Helixi | 401 – 406 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 407 – 410 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 413 – 423 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 430 – 434 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 435 – 437 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 439 – 452 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Turni | 455 – 458 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 460 – 466 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 472 – 474 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 479 – 502 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| Helixi | 506 – 510 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 513 – 524 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 537 – 551 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 553 – 559 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 562 – 565 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 566 – 568 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 569 – 571 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 576 – 578 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 584 – 586 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 589 – 593 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 599 – 612 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Turni | 620 – 622 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 637 – 640 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 645 – 666 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| Beta strandi | 667 – 669 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 676 – 678 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8RNT4 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 122 – 685 | LipoxygenasePROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 564 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the lipoxygenase family.Curated
Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4107EFQ Bacteria ENOG410YN4N LUCA |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000907 LipOase IPR013819 LipOase_C IPR036226 LipOase_C_sf IPR020834 LipOase_CS IPR020833 LipOase_Fe_BS |
The PANTHER Classification System More...PANTHERi | PTHR11771 PTHR11771, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00305 Lipoxygenase, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00087 LIPOXYGENASE |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48484 SSF48484, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00711 LIPOXYGENASE_1, 1 hit PS00081 LIPOXYGENASE_2, 1 hit PS51393 LIPOXYGENASE_3, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
Q8RNT4-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MKRRSVLLSG VALSGTALAN DSIFFSPLKY LGAEQQRSID ASRSLLDNLI
60 70 80 90 100
PPSLPQYDNL AGKLARRAVL TSKKLVYVWT ENFANVKGVP MARSVPLGEL
110 120 130 140 150
PNVDWLLKTA GVIVELIVNF VASLPASAAA QFERIAAGLS GDLEAARQVH
160 170 180 190 200
EALLEEAKND PAAAGSLLLR FTELQTRVIA LLTRVGLLVD DILKSASNLV
210 220 230 240 250
TQGGQGDGLN RFRAVFGTLR LPEVADSFRD DEAFAYWRVA GPNPLLIRRV
260 270 280 290 300
DALPANFPLG EEQFRRVMGA DDSLLEAAAS RRLYLLDYAE LGKLAPSGAV
310 320 330 340 350
DKLLTGTGFA YAPIALFALG KDRAGLLPVA IQCGQDPATH PMFVRPAESE
360 370 380 390 400
SDLYWGWQMA KTVVQVAEEN YHEMFVHLAQ THLVSEAFCL ATQRTLAPSH
410 420 430 440 450
PLHVLLAPHF EGTLFINEGA ARILLPSAGF IDVMFAAPIQ DTQATAGGNR
460 470 480 490 500
LGFDFYRGML PESLKARNVD DPAALPDYPY RDDGLLVWNA IRQWAADYVA
510 520 530 540 550
VYYASDGDVT ADVELAAWVG EVIGSGKVAG FRPITGRSQL VEVLTMVIFT
560 570 580 590 600
ASAQHAAVNF PQPSMMTYAP AICAMSAAPA PDSPSGKSEA DWLKMMPPTL
610 620 630 640 650
VALEKVNIYH LLGSVYHGRL GDYRQTGFPY APVFSDRRVT ASGGPLERFQ
660 670 680
ARLKEVEATI RTRNQARRKP YEYLLPSRIP ASTNI
Length:685
Mass (Da):74,519
Last modified:June 15, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i4F56EFE0780295FA
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF479686 Genomic DNA Translation: AAL85880.2 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:AAL85880 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8RNT4 | Lipoxygenase LoxA | ) | 685 | UniRef90_Q8RNT4 | ||
| Lipoxygenase domain-containing protein | 686 | |||||
| Oleic acid lipoxygenase | 685 | |||||
| AraC family transcriptional regulator | 685 | |||||
| Probable lipoxygenase | 685 | |||||
| +340 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8RNT4 | Lipoxygenase LoxA | ) | 685 | UniRef50_Q8RNT4 | ||
| Lipoxygenase domain-containing protein | 686 | |||||
| AraC family transcriptional regulator | 685 | |||||
| AraC family transcriptional regulator | 685 | |||||
| Oleic acid lipoxygenase | 685 | |||||
| +341 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF479686 Genomic DNA Translation: AAL85880.2 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 4G32 | X-ray | 1.75 | A | 19-685 | [»] | |
| 4G33 | X-ray | 2.03 | A | 19-685 | [»] | |
| 4RPE | X-ray | 1.60 | A | 19-685 | [»] | |
| 5LC8 | X-ray | 1.80 | A | 19-685 | [»] | |
| SMRi | Q8RNT4 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 287.DR97_765 |
Proteomic databases
| PRIDEi | Q8RNT4 |
Genome annotation databases
| KEGGi | ag:AAL85880 |
Phylogenomic databases
| eggNOGi | ENOG4107EFQ Bacteria ENOG410YN4N LUCA |
Family and domain databases
| InterProi | View protein in InterPro IPR000907 LipOase IPR013819 LipOase_C IPR036226 LipOase_C_sf IPR020834 LipOase_CS IPR020833 LipOase_Fe_BS |
| PANTHERi | PTHR11771 PTHR11771, 1 hit |
| Pfami | View protein in Pfam PF00305 Lipoxygenase, 1 hit |
| PRINTSi | PR00087 LIPOXYGENASE |
| SUPFAMi | SSF48484 SSF48484, 1 hit |
| PROSITEi | View protein in PROSITE PS00711 LIPOXYGENASE_1, 1 hit PS00081 LIPOXYGENASE_2, 1 hit PS51393 LIPOXYGENASE_3, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | LOX_PSEAI | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q8RNT4Primary (citable) accession number: Q8RNT4 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2004 |
| Last sequence update: | June 15, 2010 | |
| Last modified: | December 11, 2019 | |
| This is version 72 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
