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Q90W54 (OXLA_GLOBL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. 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=LAAO
Short name=LAO
Short name=M-LAO
EC=1.4.3.2
OrganismGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Taxonomic identifier242054 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius

Protein attributes

Sequence length504 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. Exhibits diverse biological activities, such as apoptosis, and inhibition of agonist- and shear stress-induced platelet aggregation (SIPA). 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, edema, antibacterial and antiparasitic activities. Ref.1 Ref.2

Catalytic activity

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

Cofactor

FAD.

Subunit structure

Homodimer. Ref.2

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

Signal peptide1 – 1818 Ref.1
Chain19 – 504486L-amino-acid oxidase
PRO_5000049916

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
Glycosylation3791N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 191 By similarity
Disulfide bond349 ↔ 430 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q90W54 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 17F57B46E646F12A

FASTA50457,092
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFGLQLNEF SQENDNAWYF IKNIRKRVGE VKKDPGVLKY PVKPSEEGKS AGQLYEESLG 

       190        200        210        220        230        240 
KVVEELKRTN CSYILNKYDT YSTKEYLLKE GNLSPGAVDM IGDLMNEDSG YYVSFPESLR 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVGGMDK LPTSMYRAIE EKVHLNAQVI KIQKNAEKVT VVYQTPAKEM 

       310        320        330        340        350        360 
ASVTADYVIV CTTSRATRRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDEGIH 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ 

       430        440        450        460        470        480 
LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EPLTASVDRI YFAGEHTAEA 

       490        500 
HGWIDSTIKS GLRAARDVNR ASEQ

« Hide

References

[1]"Molecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation."
Takatsuka H., Sakurai Y., Yoshioka A., Kokubo T., Usami Y., Suzuki M., Matsui T., Titani K., Yagi H., Matsumoto M., Fujimura Y.
Biochim. Biophys. Acta 1544:267-277(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-52; 62-104; 226-257; 266-299 AND 435-443, FUNCTION.
Tissue: Venom and Venom gland.
[2]"Identification of the snake venom substance that induces apoptosis."
Suhr S.M., Kim D.S.
Biochem. Biophys. Res. Commun. 224:134-139(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB072392 mRNA. Translation: BAB69450.1.

3D structure databases

ProteinModelPortalQ90W54.
SMRQ90W54. Positions 21-504.
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_GLOBL
AccessionPrimary (citable) accession number: Q90W54
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: April 3, 2013
This is version 56 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

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