Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O93364 (OXLA_CROAD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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=LAAO
Short name=LAO
EC=1.4.3.2
Alternative name(s):
Apoxin I
Apoxin-1
OrganismCrotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifier8729 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Protein attributes

Sequence length516 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 hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits 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. Ref.2

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked By similarity.

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.

Ontologies

Keywords
   Biological processApoptosis
Cytolysis
Hemolysis
   Cellular componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionAntibiotic
Antimicrobial
Hemostasis impairing toxin
Oxidoreductase
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-amino-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Chain19 – 516498L-amino-acid oxidase
PRO_0000001706

Regions

Nucleotide binding61 – 622FAD By similarity
Nucleotide binding81 – 822FAD By similarity
Nucleotide binding103 – 1064FAD By similarity
Nucleotide binding482 – 4876FAD By similarity
Nucleotide binding482 – 4832Substrate By similarity

Sites

Binding site891FAD By similarity
Binding site1061Substrate By similarity
Binding site2391Substrate By similarity
Binding site2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3901Substrate By similarity
Binding site4751FAD By similarity

Amino acid modifications

Glycosylation3791N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 189 By similarity
Disulfide bond349 ↔ 430 By similarity

Sequences

Sequence LengthMass (Da)Tools
O93364 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: FDFAA77A49FDA05A

FASTA51658,662
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG 

        70         80         90        100        110        120 
MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK 

       130        140        150        160        170        180 
FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV 

       190        200        210        220        230        240 
VEELRSTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD 

       250        260        270        280        290        300 
DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 

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

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

       430        440        450        460        470        480 
LPKEDIQTFC HPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF 

       490        500        510 
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF 

« Hide

References

[1]"Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein."
Raibekas A.A., Massey V.
Biochem. Biophys. Res. Commun. 248:476-478(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-44 AND 106-130.
Tissue: Venom and Venom gland.
[2]"On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase."
Massey V., Curti B.
J. Biol. Chem. 242:1259-1264(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071564 mRNA. Translation: AAC32267.1.
PIRJE0266.

3D structure databases

ProteinModelPortalO93364.
SMRO93364. Positions 21-503.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

InterProIPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOXLA_CROAD
AccessionPrimary (citable) accession number: O93364
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 78 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