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B5AR80 (OXLA_BOTPA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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=Bp-LAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothropoides pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis)
Taxonomic identifier1042543 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothropoides

Protein attributes

Sequence length503 AA.
Sequence statusFragment.
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 against L-Met, L-Leu, L-Phe and L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as antibacterial on both Gram-positive and Gram-negative bacteria and antiparasitic activities, 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 have activities in hemorrhage, hemolysis, edema, and apoptosis. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation. Ref.1

Miscellaneous

Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.1).

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 Ref.1
Chain19 – ›503›485L-amino-acid oxidase
PRO_0000412598

Regions

Nucleotide binding61 – 622FAD By similarity
Nucleotide binding81 – 822FAD By similarity
Nucleotide binding105 – 1084FAD By similarity
Nucleotide binding482 – 4876FAD By similarity
Nucleotide binding482 – 4832Substrate By similarity

Sites

Binding site891FAD By similarity
Binding site1081Substrate By similarity
Binding site2411Substrate By similarity
Binding site2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3901Substrate By similarity
Binding site4751FAD By similarity

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 191 By similarity
Disulfide bond349 ↔ 430 By similarity

Experimental info

Non-terminal residue5031

Sequences

Sequence LengthMass (Da)Tools
B5AR80 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 800568E8C2166CD0

FASTA50356,799
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DGNPLEECFR ETDYEEFLEI AKNGLSATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL ANAGHQVTVL EASKRAGGRV RTYRNDKEGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFGLQLNEF SQENENAWYF IKNIRKRVGE VNKDPGVLEY PVKPSEVGKS AGQLYEESLQ 

       190        200        210        220        230        240 
KAVEELRRTN CSYMLNKYDT YSTKEYLLKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVGGMDK LPTSMYQAIQ EKVRLNVRVI KIQQDVKEVT VTYQTSAKET 

       310        320        330        340        350        360 
LSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF PSGVGVIIAY GIGDDANFFQ ALDFKDCGDI VINDLSLIHQ 

       430        440        450        460        470        480 
LPKEEIQAFC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPVDRI YFAGEYTAQA 

       490        500 
HGWIDSTIKS GLTAARDVNR ASE

« Hide

References

[1]"Structural and functional properties of Bp-LAAO, a new L-amino acid oxidase isolated from Bothrops pauloensis snake venom."
Rodrigues R.S., da Silva J.F., Boldrini Franca J., Fonseca F.P., Otaviano A.R., Henrique Silva F., Hamaguchi A., Magro A.J., Braz A.S., dos Santos J.I., Homsi-Brandeburgo M.I., Fontes M.R., Fuly A.L., Soares A.M., Rodrigues V.M.
Biochimie 91:490-501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-68, FUNCTION, SUBUNIT, GLYCOSYLATION.
Tissue: Venom and Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EU870608 mRNA. Translation: ACG55578.1.

3D structure databases

ProteinModelPortalB5AR80.
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_BOTPA
AccessionPrimary (citable) accession number: B5AR80
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 23, 2008
Last modified: October 3, 2012
This is version 18 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

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