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Q4JHE1 (OXLA_PSEAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 43. 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
EC=1.4.3.2
OrganismPseudechis australis (Mulga snake) (King brown snake)
Taxonomic identifier8670 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Pseudechis

Protein attributes

Sequence length517 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, 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. This protein has antibacterial activities. Ref.2

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.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 517499L-amino-acid oxidase
PRO_5000140380

Regions

Nucleotide binding62 – 632FAD By similarity
Nucleotide binding82 – 832FAD By similarity
Nucleotide binding106 – 1094FAD By similarity
Nucleotide binding483 – 4886FAD By similarity
Nucleotide binding483 – 4842Substrate By similarity

Sites

Binding site901FAD By similarity
Binding site1091Substrate By similarity
Binding site2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3911Substrate By similarity
Binding site4761FAD By similarity

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 192 By similarity
Disulfide bond350 ↔ 431 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JHE1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 9E0ACCD728782BE5

FASTA51758,744
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRRRPLEECF READYEEFLE IAKNGLQRTS NPKRVVVVGA 

        70         80         90        100        110        120 
GMAGLSAAYV LAGAGHQVTL LEASERVGGR VNTYRNEKDG WYVNLGPMRL PERHRIIREY 

       130        140        150        160        170        180 
IRKFGLELNE FIQENDNAWY FIKNIRKRVS EVKKDPGVFK YPVKPSEEGK SASQLYRESL 

       190        200        210        220        230        240 
QKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSPGAVD MIGDLLNEDS SYYLSFIESL 

       250        260        270        280        290        300 
KSDDIFSYEK RFDEIVGGFD QLPRSMYQAI AEKVHLNAQV IKIQQNAEDV RVTYQTPAKT 

       310        320        330        340        350        360 
LSYVIADYVI VCSTSRAARR IHFEPPLPPK KAHALRSIHY RSSTKIFLTC SQKFWEADGI 

       370        380        390        400        410        420 
HGGKSTTDLP SRFIYYPNHS FTSGIGVIVA YTLADDTDFF QALDIETSAD IVINDLSLIH 

       430        440        450        460        470        480 
QLPKEQIQAL CYPSKIQKWS LDEYAMGAIT SFTPYQFQDF FEIVAAPVGR IYFAGEYTAS 

       490        500        510 
VHGWLDSTIK SGLTAARDVN LASQKPSRIQ LSNDNEL

« Hide

References

[1]"Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species."
St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.
Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom."
Stiles B.G., Sexton F.W., Weinstein S.A.
Toxicon 29:1129-1141(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ088992 mRNA. Translation: AAY89682.1.

3D structure databases

HSSPHSSP built from PDB template 2BXR based on UniProtKB P21397.
ProteinModelPortalQ4JHE1.
SMRQ4JHE1. Positions 23-505.
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_PSEAU
AccessionPrimary (citable) accession number: Q4JHE1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: August 2, 2005
Last modified: October 3, 2012
This is version 43 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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