L-amino-acid oxidase precursor - Ophiophagus hannah (King cobra)

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

Caution

The existence of two isoforms has been reported, and could explain the differences in sequence and kinetic parameters.1 Publication

Catalytic activityⁱ

Cofactorⁱ

FAD2 Publications

Kineticsⁱ

Temperature dependenceⁱ

Exhibits unusual thermal stability. At pH 7.4, the enzyme retains full activity after incubation at 25 degrees Celsius for 30 days. Is stable at alkaline condition and is not inactivated by freezing.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	89	FADBy similarity	1
Binding siteⁱ	106	SubstrateBy similarity	1
Binding siteⁱ	269	FAD; via amide nitrogen and carbonyl oxygenBy similarity	1
Binding siteⁱ	380	SubstrateBy similarity	1
Binding siteⁱ	465	FADBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	61 – 62	FADBy similarity	2
Nucleotide bindingⁱ	81 – 82	FADBy similarity	2
Nucleotide bindingⁱ	103 – 106	FADBy similarity	4
Nucleotide bindingⁱ	472 – 477	FADBy similarity	6

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

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

BRENDAⁱ	1.4.3.2, 4419
SABIO-RKⁱ	P81383

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: L-amino-acid oxidase1 Publication (EC:1.4.3.22 Publications) Short name: LAO Short name: Oh-LAAO1 Publication
Organismⁱ	Ophiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifierⁱ	8665 [NCBI]
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

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Toxic doseⁱ

LD₅₀ is 5 mg/kg by intravenous injection into mice.1 Publication

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 20	3 PublicationsAdd BLAST		20
ChainⁱPRO_0000099871	21 – 491	L-amino-acid oxidase3 PublicationsAdd BLAST		471

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	28 ↔ 182	By similarity
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
Glycosylationⁱ	410	N-linked (GlcNAc...) asparagineSequence analysis	1

Post-translational modificationⁱ

N-glycosylated.4 Publications

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEⁱ	P81383
TopDownProteomicsⁱ	P81383

Expressionⁱ

Tissue specificityⁱ

Expressed by the venom gland.1 Publication

Interactionⁱ

Subunit structureⁱ

Homodimer; non-covalently linked.

4 Publications

Structureⁱ

3D structure databases

SMRⁱ	P81383
ModBaseⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	472 – 473	Substrate bindingBy similarity		2

Sequence similaritiesⁱ

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.Curated

Keywords - Domainⁱ

Signal

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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01593, Amino_oxidase, 1 hit
PRINTSⁱ	PR00757, AMINEOXDASEF
SUPFAMⁱ	SSF51905, SSF51905, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P81383-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:491

Mass (Da):55,977

Last modified:September 21, 2011 - v3

Checksum:ⁱ2FD1E740BD73313E

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
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: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	EF080831 mRNA Translation: ABN72538.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

EF080831 mRNA Translation: ABN72538.1

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P81383	Amine oxidase (Fragment)		OPHHA		489	UniRef90_P81383

Protein	Similar proteins		Species	Score	Length	Source
P81383	Amine oxidase (Fragment)		OPHHA		489	UniRef50_P81383
Uncharacterized protein		northern spotted owl		544
Uncharacterized protein		Pink-footed goose		525
Uncharacterized protein		ANSCY		511
Amine oxidase (Fragment)		ANSSE		499
+39

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	EF080831 mRNA Translation: ABN72538.1

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
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	OXLA_OPHHA
Accessionⁱ	P81383Primary (citable) accession number: P81383 Secondary accession number(s): A8QL50
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.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Animal Toxin Annotation Program
Annotation program	Chordata Protein Annotation Program

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UniParc

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Supporting data

UniProtKB - P81383 (OXLA_OPHHA)

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L-amino-acid oxidase

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<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

Caution

<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

<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

Temperature dependencei

Sites

Regions

<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

GO - Biological processi

Enzyme and pathway databases

<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 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

Extracellular region or secreted

Keywords - Cellular componenti

<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 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

Amino acid modifications

Keywords - PTMi

Proteomic databases

<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 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 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

<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

<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

Family and domain databases

Experimental Info

Sequence databases

<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

3D structure databases

Proteomic databases

Enzyme and pathway databases

Family and domain databases

<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 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

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Temperature dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ