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Reviewed, UniProtKB/Swiss-Prot Q90W54 (OXLA_AGKHA)

Last modified November 25, 2008. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    L-amino acid oxidase
    EC=1.4.3.2
Alternative name(s):
    M-LAO
    LAAO
      Short name=LAO
OrganismAgkistrodon halys blomhoffi (Mamushi) (Gloydius blomhoffii)
Taxonomic identifier242054 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius

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Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Has an ability to induce hemorrhage and has an antibacterial activity By similarity. Has an ability to induce apoptosis. Inhibits both agonist- and shear stress-induced platelet aggregation (SIPA) dose-dependently.

Catalytic activity

An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).

Cofactor

FAD.

Subunit structure

Homodimer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Nucleotide binding107 – 1082FAD
Nucleotide binding484 – 4874FAD

Sites

Binding site621FAD
Binding site811FAD
Binding site891FAD
Binding site1081Substrate
Binding site2411Substrate
Binding site2791FAD; via amide nitrogen and carbonyl oxygen
Binding site3901Substrate
Binding site4751FAD

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...)
Glycosylation3791N-linked (GlcNAc...)
Disulfide bond28 ↔ 191
Disulfide bond349 ↔ 430

Secondary structure

1 ................................................................................................ 504
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q90W54-1 [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

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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: 11341935] [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: 8694800] [Abstract]
Cited for: FUNCTION, SUBUNIT.
Tissue: Venom.
[3]"Structures of L-amino acid oxidase in complex with substrates and substrate analogue."
Zhang H., Teng M., Niu L.
Submitted (MAY-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-504, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379, INTERACTION WITH COFACTOR AND SUBSTRATE ANALOGS.

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Cross-references

Sequence databases

AB072392 mRNA. Translation: BAB69450.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TDKX-ray2.70A19-504[»]
1TDNX-ray2.70A19-504[»]
1TDOX-ray3.00A19-504[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENQ90W54.

Family and domain databases

InterProIPR000759. Adrndx_reductase.
IPR001613. Amineoxid_fl.
IPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00419. ADXRDTASE.
PR00757. AMINEOXDASEF.
ProtoNetSearch...

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Entry information

Entry nameOXLA_AGKHA
AccessionPrimary (citable) accession number: Q90W54
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: November 25, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families