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A8QL52 (OXLA_BUNFA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 29. 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=Bf-LAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBungarus fasciatus (Banded krait)
Taxonomic identifier8613 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Protein attributes

Sequence length517 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 (highly active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active against L-Lys, L-Arg, L-Ala and L-Asn), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as edema, inflammatory cell infiltration, cytotoxicity and apoptosis, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, and have antibacterial and antiparasitic activities. Ref.2

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=28.28 mM for L-Ala Ref.2

KM=18.75 mM for L-Arg

KM=0.04 mM for L-Asp

KM=19.07 mM for L-Asn

KM=5.88 mM for L-Gln

KM=1.44 mM for L-Glu

KM=4.84 mM for L-His

KM=1.64 mM for L-Ile

KM=60.69 mM for L-Leu

KM=21.49 mM for L-Lys

KM=15.03 mM for L-Met

KM=0.13 mM for L-Phe

KM=0.27 mM for L-Trp

KM=0.05 mM for L-Tyr

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 517498L-amino-acid oxidase
PRO_0000412599

Regions

Nucleotide binding62 – 632FAD By similarity
Nucleotide binding82 – 832FAD By similarity
Nucleotide binding106 – 1094FAD By similarity
Nucleotide binding483 – 4886FAD By similarity
Nucleotide binding483 – 4842Substrate By similarity

Sites

Binding site901FAD By similarity
Binding site1091Substrate By similarity
Binding site2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3911Substrate By similarity
Binding site4761FAD By similarity

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 192 By similarity
Disulfide bond350 ↔ 431 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8QL52 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: E869950FB941B11D

FASTA51758,764
        10         20         30         40         50         60 
MNVFSIFSLV FLAAFGSCAD DRRSALEECF READYEEFLE IARNGLKKTS NPKHVVVVGA 

        70         80         90        100        110        120 
GMAGLSAAYV LAGAGHRVTL LEASDRVGGR VNTYRDEKEG WYVNMGPMRL PERHRIVRTY 

       130        140        150        160        170        180 
IAKFGLKLNE FFQENENAWY FIRNIRKRVW EVKKDPGVFK YPVKPSEEGK SASQLYRESL 

       190        200        210        220        230        240 
KKVIEELKRT NCSYILDKYD TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL 

       250        260        270        280        290        300 
KNDDLFSYEK RFDEISDGFD QLPKSMHQAI AEMVHLNAQV IKIQRDAEKV RVAYQTPAKT 

       310        320        330        340        350        360 
LSYVTADYVI VCATSRAVRR ISFEPPLPPK KAHALRSIHY KSATKIFLTC TRKFWEADGI 

       370        380        390        400        410        420 
HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YVLADDSDFF QALDIKTSAD IVINDLSLIH 

       430        440        450        460        470        480 
QLPKNEIQAL CYPSLIKKWS LDKYTMGALT SFTPYQFQDY IETVAAPVGR IYFAGEYTAT 

       490        500        510 
VHGWLDSTIK SGLTAARNVN RASQKPSRIH LINDNQL 

« 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].
Tissue: Venom gland.
[2]"Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom."
Wei J.-F., Yang H.-W., Wei X.-L., Qiao L.-Y., Wang W.-Y., He S.-H.
Toxicon 54:262-271(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-36, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF080833 mRNA. Translation: ABN72540.1.

3D structure databases

ProteinModelPortalA8QL52.
SMRA8QL52. Positions 23-505.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

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_BUNFA
AccessionPrimary (citable) accession number: A8QL52
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families