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Reviewed, UniProtKB/Swiss-Prot Q6STF1 (OXLA_AGKHP)

Last modified June 16, 2009. Version 31. 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

Names and origin

Protein namesRecommended name:
    L-amino-acid oxidase
      Short name=LAAO
      Short name=LAO
      Short name=AHP-LAAO
    EC=1.4.3.2
OrganismAgkistrodon halys pallas (Chinese water mocassin) (Gloydius halys pallas)
Taxonomic identifier8714 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeGloydius

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. Inhibits platelet aggregation and has an ability to induce hemorrhage. Has an antibacterial activity By similarity. Induces apoptosis of cultured HeLa cells.

Catalytic activity

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 504486L-amino-acid oxidase
PRO_0000273563

Regions

Nucleotide binding107 – 1082FAD
Nucleotide binding475 – 48713FAD

Sites

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

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Ref.2
Glycosylation3791N-linked (GlcNAc...) Ref.2
Disulfide bond28 ↔ 191 Ref.2
Disulfide bond349 ↔ 430 Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6STF1-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: AEB034155184F0A7

FASTA50457,125
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAN DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVVVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEDW 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 ESLTASVDRI YFAGEHTAEA 

       490        500 
HGWIDSTIKS GLRAARDVNR ASEQ 

« Hide

References

[1]Zhang H., Zhang T., Teng M., Niu L.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom."
Zhang H., Teng M., Niu L., Wang Y., Wang Y., Liu Q., Huang Q., Hao Q., Dong Y., Liu P.
Acta Crystallogr. D 60:974-977(2004) [PubMed: 15103157] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 19-504, PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379, FUNCTION, MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

Sequence databases

AY450403 mRNA. Translation: AAR20248.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1REOX-ray2.31A19-504[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENQ6STF1.

Enzyme and pathway databases

BRENDA1.4.3.2. 95980.

Family and domain databases

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

Entry information

Entry nameOXLA_AGKHP
AccessionPrimary (citable) accession number: Q6STF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents