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Q6WP39 (OXLA_TRIST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 45. 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=TSV-LAO
EC=1.4.3.2
OrganismTrimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Taxonomic identifier39682 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Viridovipera

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. 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.

Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication.

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 By similarity.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated. 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 By similarity
Chain19 – 516498L-amino-acid oxidase
PRO_0000273572

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

Experimental info

Sequence conflict161G → E in AAQ16182. Ref.2
Sequence conflict531H → R in AAQ16182. Ref.2
Sequence conflict731A → T in AAQ16182. Ref.2
Sequence conflict1811K → E in AAQ16182. Ref.2
Sequence conflict2941H → Q in AAQ16182. Ref.2
Sequence conflict3151R → G in AAQ16182. Ref.2
Sequence conflict3541R → W in AAQ16182. Ref.2
Sequence conflict5141D → N in AAQ16182. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6WP39 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FB5AC0BC171B9288

FASTA51658,601
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFNLQLNEF SQENDNAWHF VKNIRKTVGE VKKDPGVLKY PVKPSEEGKS AEQLYEESLR 

       190        200        210        220        230        240 
KVEKELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT 

       310        320        330        340        350        360 
SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT KKFREDEGIH 

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

       430        440        450        460        470        480 
LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EALTSHVDRI YFAGEYTAHA 

       490        500        510 
HGWIDSSIKS GLTAARDVNR ASENPSGIHL SNDDEL

« Hide

References

[1]"Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity."
Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y.
Biochem. Biophys. Res. Commun. 309:598-604(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY.
Tissue: Venom and Venom gland.
[2]"Purification, cloning and characterization of the L-amino acid oxidase in snake Trimeresurus stejnegeri."
Wang J., Huang Q., Teng M., Niu L.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY277739 mRNA. Translation: AAQ56232.1.
AY338966 mRNA. Translation: AAQ16182.1.

3D structure databases

HSSPHSSP built from PDB template 1F8R based on UniProtKB P81382.
ProteinModelPortalQ6WP39.
SMRQ6WP39. Positions 21-503.
ModBaseSearch...

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_TRIST
AccessionPrimary (citable) accession number: Q6WP39
Secondary accession number(s): Q7T062
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 45 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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