UniProtKB - P81383 (OXLA_OPHHA)
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>sp|P81383|OXLA_OPHHA L-amino-acid oxidase OS=Ophiophagus hannah OX=8665 PE=1 SV=3 MNDFLLLLLVLFLGVPRSENHVINLEECFQEPEYENWLATASHGLTKTLNPKKIVIVGAG ISGLTAAKLFREAGHEVVILEASDRVGGRIKTHREDGWYVDVGPMRVPQTHRIVREYIKK FNISLNPFRQTDENAWYLIKHVRQKMSANNPENFGYQLNPNERGKSASQLFDETLDKVTD DCTLQKEKYDSFSTKEYLIKEGKLSTGAVEMIGDFLNEEAGFHNSFLISVMDHFLFLNNS FDEITGGFDQLPERFFKDMDSIVHLNSTVEKIVHINNKVTVFYEGLSTNMRLVADYVLIT ATARATRLIKFVPPLSIPKTRALRSLIYASATKIILVCTDKFWEKDGIHGGRSITDLPSR VIYYPNHDFTNGIGVLLASYTWYSDSEFYTTLSDEKCVDVVMDDLVEIHNVSKDYLKSVC GKHVVQKWALDQYSMGAFSTYTPYQITHYSQMLAQNEGRIYFAGEYTAHPHGWIETSMKS AIREAINIHNACommunity curation ()Add a publicationFeedback
L-amino-acid oxidase
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
Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:17543361, PubMed:2044840).
Is very active against L-Lys, L-Phe, L-Leu, L-Tyr, L-Trp, L-Arg, and L-Met, moderately active against L-His, L-cystine, and L-Ile, and slightly active against L-Gln, L-Asn, L-Ala, and L-Val (PubMed:2044840).
L-Glu, L-Ser, L-Pro and Gly are oxidized very slowly (PubMed:2044840).
Its activity on platelet aggregation is controversial. It has potent inhibitory activity on platelet aggregation induced by ADP and the thromboxane analog U46619, but not by thrombin, mucetin, ristocetin and stejnulxin (PubMed:17543361), but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide (PubMed:7886693).
It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.
6 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"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract] - Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION. - Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE. - Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.7"Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation."
Li Z.Y., Yu T.F., Lian E.C.
Toxicon 32:1349-1358(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.8"Antibacterial action of a heat-stable form of L-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom."
Lee M.L., Tan N.H., Fung S.Y., Sekaran S.D.
Comp. Biochem. Physiol. 153:237-242(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ANTIBACTERIAL ACTIVITY.
Caution
<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.6"The edema inducing activity of Ophiophagus hannah (king cobra) venom L-amino acid oxidase."
Tan N.-H., Choy S.-K.
Toxicon 32:539-539(1994)Cited for: ISOFORM.
<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
- an L-α-amino acidEC:1.4.3.2
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Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract] - Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract] - Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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=3-(4-hydroxyphenyl)pyruvate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O2- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+NH4+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
- H2O
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+L-cystine- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+O2- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=(2R)-2-amino-2-carboxylatoethyl-disulfanyl-oxopropanoate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+H2O2- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+NH4+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
- H2O
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+L-lysine- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+O2- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=6-amino-2-oxohexanoate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+H2O2- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+NH4+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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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
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.2"Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
Ponnudurai G., Chung M.C.M., Tan N.-H.
Arch. Biochem. Biophys. 313:373-378(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-39, SUBUNIT, GLYCOSYLATION, COFACTOR. - Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
<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
- KM=2.3 mM for L-His1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
- KM=3.0 mM for L-His1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=2.9 mM for L-Ile1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
- KM=1.3 mM for L-Ile1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=2.2 mM for L-Leu1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
- KM=0.20 mM for L-Leu1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=2.6 mM for L-Lys1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
- KM=0.14 mM for L-Lys1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.7 mM for L-Met1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
- KM=0.01 mM for L-Tyr1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.10 mM for L-Trp1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.10 mM for L-Phe1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.15 mM for L-Arg1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.17 mM for L-ornithine1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.35 mM for L-norleucine (L-2-aminohexanoate)1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.63 mM for L-Met1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.67 mM for L-norvaline (L-2-aminopentanoate)1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=0.83 mM for L-cystine1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=4.0 mM for L-Aminobutyric acid1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=5.0 mM for L-Pro1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=7.1 mM for L-Val1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=7.8 mM for L-Glu1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=12.5 mM for L-Ala1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=20.0 mM for L-Gln1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=22.2 mM for L-Asn1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=28.6 mM for L-Ser1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- KM=31.0 mM for L-Gly1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Temperature dependencei
Manual assertion based on experiment ini
- Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
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 describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 89 | FADBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
Binding sitei | 106 | SubstrateBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Binding sitei | 269 | FAD; via amide nitrogen and carbonyl oxygenBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Binding sitei | 380 | SubstrateBy similarity | 1 | |
Binding sitei | 465 | FADBy similarity Manual assertion inferred from sequence similarity toi | 1 |
Regions
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 describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 61 – 62 | FADBy similarity Manual assertion inferred from sequence similarity toi | 2 | |
Nucleotide bindingi | 81 – 82 | FADBy similarity Manual assertion inferred from sequence similarity toi | 2 | |
Nucleotide bindingi | 103 – 106 | FADBy similarity Manual assertion inferred from sequence similarity toi | 4 | |
Nucleotide bindingi | 472 – 477 | FADBy similarity Manual assertion inferred from sequence similarity toi | 6 |
<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
- DNA binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION.
- flavin adenine dinucleotide binding Source: UniProtKBInferred from direct assayi
- Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
- L-amino-acid oxidase activity Source: UniProtKBInferred from direct assayi
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract] - Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION.
- L-lysine oxidase activity Source: RHEA
- L-phenylalaine oxidase activity Source: RHEA
- toxin activity Source: UniProtKBInferred from direct assayi
- Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION.
GO - Biological processi
- apoptotic process Source: UniProtKB-KW
- defense response to bacterium Source: UniProtKB-KW
- hemolysis in other organism Source: UniProtKB-KW
- killing of cells of other organism Source: UniProtKBInferred from direct assayi
- Ref.8"Antibacterial action of a heat-stable form of L-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom."
Lee M.L., Tan N.H., Fung S.Y., Sekaran S.D.
Comp. Biochem. Physiol. 153:237-242(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ANTIBACTERIAL ACTIVITY. - Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION.
- modulation of process of other organism Source: UniProtKBInferred from direct assayi
- Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
<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 | Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin |
Biological process | Apoptosis, Cytolysis, Hemolysis |
Ligand | FAD, Flavoprotein |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.4.3.2, 4419 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P81383 |
<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: L-amino-acid oxidase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: LAO Short name: Oh-LAAO1 Publication Manual assertion based on opinion ini
|
<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 | Ophiophagus hannah (King cobra) (Naja hannah) |
<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 | 8665 [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 › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Elapidae › Elapinae › Ophiophagus |
<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
Extracellular region or secreted
- Secreted 1 Publication
Manual assertion based on experiment ini
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKBInferred from direct assayi
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
- extracellular region Source: UniProtKBInferred from direct assayi
Keywords - Cellular componenti
Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the lethal dose (LD), paralytic dose (PD), effect dose (ED) or lethal concentration (LC) of a protein toxin.<p><a href='/help/toxic_dose' target='_top'>More...</a></p>Toxic dosei
Manual assertion based on experiment ini
- Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
<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 – 20 | 3 Publications Manual assertion based on experiment ini
| 20 | |
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000099871 | 21 – 491 | L-amino-acid oxidase3 Publications Manual assertion inferred by curator fromi
| 471 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 28 ↔ 182 | By similarity Manual assertion inferred from sequence similarity toi | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 122 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 238 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 266 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 338 ↔ 420 | By similarity Manual assertion inferred from sequence similarity toi | ||
Glycosylationi | 410 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Manual assertion inferred by curator fromi
- Ref.1"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract] - Ref.2"Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
Ponnudurai G., Chung M.C.M., Tan N.-H.
Arch. Biochem. Biophys. 313:373-378(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-39, SUBUNIT, GLYCOSYLATION, COFACTOR. - Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION. - Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PRoteomics IDEntifications database More...PRIDEi | P81383 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P81383 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Manual assertion inferred by curator fromi
- Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
<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
Homodimer; non-covalently linked.
4 PublicationsManual assertion based on experiment ini
- Ref.2"Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
Ponnudurai G., Chung M.C.M., Tan N.-H.
Arch. Biochem. Biophys. 313:373-378(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-39, SUBUNIT, GLYCOSYLATION, COFACTOR. - Ref.3"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
Ahn M.Y., Lee B.M., Kim Y.S.
Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION. - Ref.4"Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
Tan N.H., Saifuddin M.N.
Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE. - Ref.5"Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
Tan N.H., Saifuddin M.N.
Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
<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
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P81383 |
Database of comparative protein structure models More...ModBasei | 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
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 472 – 473 | Substrate bindingBy similarity Manual assertion inferred from sequence similarity toi | 2 |
<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
Keywords - Domaini
SignalFamily and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.50.50.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002937, Amino_oxidase IPR036188, FAD/NAD-bd_sf IPR001613, Flavin_amine_oxidase |
Pfam protein domain database More...Pfami | View protein in Pfam PF01593, Amino_oxidase, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00757, AMINEOXDASEF |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51905, SSF51905, 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.
10 20 30 40 50
MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN
60 70 80 90 100
PKKIVIVGAG ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV
110 120 130 140 150
DVGPMRVPQT HRIVREYIKK FNISLNPFRQ TDENAWYLIK HVRQKMSANN
160 170 180 190 200
PENFGYQLNP NERGKSASQL FDETLDKVTD DCTLQKEKYD SFSTKEYLIK
210 220 230 240 250
EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS FDEITGGFDQ
260 270 280 290 300
LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT
310 320 330 340 350
ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG
360 370 380 390 400
GRSITDLPSR VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV
410 420 430 440 450
VMDDLVEIHN VSKDYLKSVC GKHVVQKWAL DQYSMGAFST YTPYQITHYS
460 470 480 490
QMLAQNEGRI YFAGEYTAHP HGWIETSMKS AIREAINIHN A
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 21 | H → S AA sequence (PubMed:9304806).Curated | 1 | |
Sequence conflicti | 28 | C → S AA sequence (PubMed:8080286).Curated | 1 | |
Sequence conflicti | 28 | C → S AA sequence (PubMed:9304806).Curated | 1 | |
Sequence conflicti | 37 | W → H AA sequence (PubMed:8080286).Curated | 1 |
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 | EF080831 mRNA Translation: ABN72538.1 |
<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 | |
---|---|---|---|---|---|---|
P81383 | Amine oxidase (Fragment) | 489 | UniRef90_P81383 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P81383 | Amine oxidase (Fragment) | 489 | UniRef50_P81383 | |||
Uncharacterized protein | 544 | |||||
Uncharacterized protein | 525 | |||||
Uncharacterized protein | 511 | |||||
Amine oxidase (Fragment) | 499 | |||||
+39 |
<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 | EF080831 mRNA Translation: ABN72538.1 |
3D structure databases
SMRi | P81383 |
ModBasei | Search... |
Proteomic databases
PRIDEi | P81383 |
TopDownProteomicsi | P81383 |
Enzyme and pathway databases
BRENDAi | 1.4.3.2, 4419 |
SABIO-RKi | P81383 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002937, Amino_oxidase IPR036188, FAD/NAD-bd_sf IPR001613, Flavin_amine_oxidase |
Pfami | View protein in Pfam PF01593, Amino_oxidase, 1 hit |
PRINTSi | PR00757, AMINEOXDASEF |
SUPFAMi | SSF51905, SSF51905, 1 hit |
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 | OXLA_OPHHA | |
<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 | P81383Primary (citable) accession number: P81383 Secondary accession number(s): A8QL50 | |
<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: | December 15, 1998 |
Last sequence update: | September 21, 2011 | |
Last modified: | April 7, 2021 | |
This is version 84 of the entry and version 3 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 | Animal Toxin Annotation Program | |
Annotation program | Chordata 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
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families