Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8QL51 (OXLA_BUNMU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 25. 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
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=Bm-LAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBungarus multicinctus (Many-banded krait)
Taxonomic identifier8616 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation 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 By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked By similarity.

Subcellular location

Secreted By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 517499L-amino-acid oxidase
PRO_0000412600

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
A8QL51 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: A9F28766C1B3AB97

FASTA51758,811
        10         20         30         40         50         60 
MNVFSIFSLV FLAAFGSCAD DRRSPLEECF READYEEFLE IARNGLKKTS NPKHVVVVGA 

        70         80         90        100        110        120 
GMAGLSAAYV LEKAGHRVTL LEASDRVGGR ANTYRDEKEG WYVNMGPMRL PERHRIVRTY 

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

       190        200        210        220        230        240 
KKIIEELKRT NCSYILDKYD SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL 

       250        260        270        280        290        300 
KNDDLFSYEK RFDEISGGFD QLPKSMHQDI AEMVHLNAQV TKIQHDAEKV RVAYQTPAKT 

       310        320        330        340        350        360 
LSYVTADYVI VCATSRAVRR ISFEPPLPSK KAHALRSIHY KSATKIFLTC TQKFWEADGI 

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

       430        440        450        460        470        480 
QLPKNEIQAL CYPSLIKKWS LDKYTMGALT SFTPYQFQDY SETVAAPVGR IYFAGEYTAR 

       490        500        510 
VHGWLDSTIK SGLTAARDVN RASQKPSRIH LISDNQL

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EF080832 mRNA. Translation: ABN72539.1.

3D structure databases

ProteinModelPortalA8QL51.
SMRA8QL51. Positions 23-505.
ModBaseSearch...

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_BUNMU
AccessionPrimary (citable) accession number: A8QL51
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 15, 2008
Last modified: October 3, 2012
This is version 25 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents