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P0DI84 (OXLA_VIPAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase
Short name=LAAO
Short name=LAO
Short name=VAA-LAAO I
EC=1.4.3.2
OrganismVipera ammodytes ammodytes (Western sand viper)
Taxonomic identifier8705 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Vipera ›

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
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. 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. Ref.3

Subunit structure

Homodimer; non-covalently linked. Ref.3

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484L-amino-acid oxidase
PRO_0000412591

Regions

Nucleotide binding41 – 422FAD
Nucleotide binding61 – 622FAD
Nucleotide binding85 – 884FAD
Nucleotide binding462 – 4676FAD
Nucleotide binding462 – 4632Substrate By similarity
Nucleotide binding464 – 4674FAD

Sites

Metal binding731Zinc
Metal binding2771Zinc
Binding site691FAD
Binding site881Substrate By similarity
Binding site2211Substrate By similarity
Binding site2591FAD; via amide nitrogen and carbonyl oxygen
Binding site3701Substrate By similarity
Binding site4551FAD

Amino acid modifications

Glycosylation1701N-linked (GlcNAc...) Ref.3
Disulfide bond8 ↔ 171 Ref.3
Disulfide bond329 ↔ 410 Ref.3

Sequences

Sequence LengthMass (Da)Tools
P0DI84 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: FF2BBFB0EB5D1C47

FASTA48454,748
        10         20         30         40         50         60 
DRNPLEECFR ETDYEEFLEI ARNGLKKTSN PKHVVVVGAG MSGLSAAYVL AGAGHKVTVL 

        70         80         90        100        110        120 
EASERAGGRV RTHRNSKEGW YANLGPMRIP EKHRIVREYI RKFGLNLNEF SQENDNAWYF 

       130        140        150        160        170        180 
IKNIRKRVGE VNKDPGLLKY PVKPSEEGKS AGQLYEESLG SAVKDLKRTN CSYILNKYDT 

       190        200        210        220        230        240 
YSTKEYLIKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR FDEIVGGMDQ 

       250        260        270        280        290        300 
LPTSMYRAIE EKVKFNARVI KIQQNANQVT VTYQTPEKDT SSNTADYVIV CTTSRAARRI 

       310        320        330        340        350        360 
QFEPPLPPKK QHALRSVHYR SGTKIFLTCS SKFWEDDGIH GGKSTTDLPS RFIYYPNHNF 

       370        380        390        400        410        420 
STGVGVIIAY GIGDDANFFQ ALKFKDCADI VFNDLSLIHQ LPKEEIQSFC YPSMIQKWSL 

       430        440        450        460        470        480 
DKYAMGAITT FTPYQFQRFS EALTAPQGRI FFAGEYTAEA HGWIDSTIKS GLTAARDVNR 


ASEQ

« Hide

References

[1]"Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom."
Georgieva D., Kardas A., Buck F., Perbandt M., Betzel C.
Acta Crystallogr. F 64:918-921(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION.
Tissue: Venom.
[2]"Comparative analysis of the venom proteomes of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis."
Georgieva D., Risch M., Kardas A., Buck F., von Bergen M., Betzel C.
J. Proteome Res. 7:866-886(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Venom.
[3]"The structure of a native L-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions."
Georgieva D., Murakami M., Perband M., Arni R., Betzel C.
Mol. Biosyst. 7:379-384(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH FAD AND ZINC IONS, COFACTOR, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-170.
Tissue: Venom.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KVEX-ray2.57A/B/C/D1-484[»]
ProteinModelPortalP0DI84.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Other

EvolutionaryTraceP0DI84.

Entry information

Entry nameOXLA_VIPAA
AccessionPrimary (citable) accession number: P0DI84
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: May 29, 2013
This is version 9 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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