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Q6STF1 (OXLA_GLOHA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=AHP-LAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismGloydius halys (Chinese water mocassin) (Agkistrodon halys)
Taxonomic identifier8714 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius

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, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, 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. This protein induces apoptosis of cultured HeLa cells. Ref.2

Catalytic activity

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

Cofactor

FAD.

Subunit structure

Homodimer; non-covalently linked.

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 binding61 – 622FAD
Nucleotide binding81 – 822FAD
Nucleotide binding105 – 1084FAD
Nucleotide binding482 – 4876FAD
Nucleotide binding482 – 4832Substrate

Sites

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

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Ref.2 Ref.3
Glycosylation3791N-linked (GlcNAc...) Ref.2 Ref.3
Disulfide bond28 ↔ 191 Ref.2 Ref.3
Disulfide bond349 ↔ 430 Ref.2 Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6STF1 [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 19-504 IN COMPLEX WITH FAD, PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379, FUNCTION, MASS SPECTROMETRY.
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 IN COMPLEX WITH FAD AND SUBSTRATE ANALOGS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY450403 mRNA. Translation: AAR20248.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1REOX-ray2.31A19-504[»]
1TDKX-ray2.70A19-504[»]
1TDNX-ray2.70A19-504[»]
1TDOX-ray3.00A19-504[»]
ProteinModelPortalQ6STF1.
SMRQ6STF1. Positions 21-504.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ6STF1.

Entry information

Entry nameOXLA_GLOHA
AccessionPrimary (citable) accession number: Q6STF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: March 6, 2013
This is version 49 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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