Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P81383 (OXLA_OPHHA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
Short name=Oh-LAAO
EC=1.4.3.2
OrganismOphiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifier8665 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeOphiophagus

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Unlike most snake L-amino-acid oxidases, this enzyme exhibits potent activity against L-Lys. Has also potent activity against L-Met, L-Leu, L-His, L-Lys and L-Ile. 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 (Ref.1), but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide (Ref.7). 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. Ref.3 Ref.4 Ref.5 Ref.7 Ref.8

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD. Ref.2 Ref.4

Subunit structure

Homodimer; non-covalently linked. Ref.2 Ref.3 Ref.4 Ref.5

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated Probable. Ref.1 Ref.2 Ref.3 Ref.4

Toxic dose

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

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Caution

The existence of two isoforms has been reported (Ref.6), and could explain the differences in sequence and kinetic parameters.

Biophysicochemical properties

Kinetic parameters:

KM=2.3 mM for L-His (Ref.1) Ref.1 Ref.4 Ref.5

KM=2.9 mM for L-Ile (Ref.1)

KM=2.2 mM for L-Leu (Ref.1)

KM=2.6 mM for L-Lys (Ref.1)

KM=0.7 mM for L-Met (Ref.1)

KM=0.20 mM for L-Leu (Ref.5)

KM=0.63 mM for L-Met (Ref.5)

KM=0.10 mM for L-Phe (Ref.5)

KM=0.10 mM for L-Trp (Ref.5)

Temperature dependence:

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1 Ref.2 Ref.3
Chain21 – 491471L-amino-acid oxidase
PRO_0000099871

Regions

Nucleotide binding61 – 622FAD By similarity
Nucleotide binding81 – 822FAD By similarity
Nucleotide binding103 – 1064FAD By similarity
Nucleotide binding472 – 4776FAD By similarity
Nucleotide binding472 – 4732Substrate By similarity

Sites

Binding site891FAD By similarity
Binding site1061Substrate By similarity
Binding site2691FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3801Substrate By similarity
Binding site4651FAD By similarity

Amino acid modifications

Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 182 By similarity
Disulfide bond338 ↔ 420 By similarity

Experimental info

Sequence conflict211H → S AA sequence Ref.3
Sequence conflict281C → S AA sequence Ref.2
Sequence conflict281C → S AA sequence Ref.3
Sequence conflict371W → H AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P81383 [UniParc].

Last modified September 21, 2011. Version 3.
Checksum: 2FD1E740BD73313E

FASTA49155,977
        10         20         30         40         50         60 
MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN PKKIVIVGAG 

        70         80         90        100        110        120 
ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV DVGPMRVPQT HRIVREYIKK 

       130        140        150        160        170        180 
FNISLNPFRQ TDENAWYLIK HVRQKMSANN PENFGYQLNP NERGKSASQL FDETLDKVTD 

       190        200        210        220        230        240 
DCTLQKEKYD SFSTKEYLIK EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS 

       250        260        270        280        290        300 
FDEITGGFDQ LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT 

       310        320        330        340        350        360 
ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG GRSITDLPSR 

       370        380        390        400        410        420 
VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV VMDDLVEIHN VSKDYLKSVC 

       430        440        450        460        470        480 
GKHVVQKWAL DQYSMGAFST YTPYQITHYS QMLAQNEGRI YFAGEYTAHP HGWIETSMKS 

       490 
AIREAINIHN A 

« Hide

References

[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]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45; 121-129; 189-195; 272-278 AND 428-439, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
Tissue: Venom and Venom gland.
[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.
Tissue: Venom.
[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.
Tissue: Venom.
[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.
[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.
Tissue: Venom.
[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.
[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.
Tissue: Venom.
[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.
Tissue: Venom.
[9]"The king cobra genome reveals dynamic gene evolution and adaptation in the snake venom system."
Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., de Koning A.P., Pollock D.D., Yandell M. expand/collapse author list , Calderon D., Renjifo C., Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.
Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF080831 mRNA. Translation: ABN72538.1.

3D structure databases

ProteinModelPortalP81383.
SMRP81383. Positions 25-491.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Enzyme and pathway databases

SABIO-RKP81383.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameOXLA_OPHHA
AccessionPrimary (citable) accession number: P81383
Secondary accession number(s): A8QL50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families