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Reviewed, UniProtKB/Swiss-Prot P81382 (OXLA_AGKRH)

Last modified November 24, 2009. Version 67. 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
      Short name=LAAO
      Short name=LAO
    EC=1.4.3.2
OrganismAgkistrodon rhodostoma (Malayan pit viper) (Calloselasma rhodostoma)
Taxonomic identifier8717 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Calloselasma

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Protein attributes

Sequence length516 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. Inhibits platelet aggregation. Has an ability to induce apoptosis and hemorrhage. Has an antibacterial activity By similarity.

Catalytic activity

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

Cofactor

FAD.

Subunit structure

Homodimer. Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

This protein constitutes 30% of the venom.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.63 mM for L-Leu

KM=0.24 mM for L-Met

KM=0.08 mM for L-Trp

pH dependence:

Optimum pH is 9.0.

Temperature dependence:

Thermostable.

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Ontologies

Keywords
   Biological processApoptosis
Blood coagulation
   Cellular componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionAntibiotic
Antimicrobial
Oxidoreductase
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-amino-acid oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2 Ref.1
Chain19 – 516498L-amino-acid oxidase
PRO_0000001707

Regions

Nucleotide binding43 – 442FAD
Nucleotide binding63 – 719FAD
Nucleotide binding89 – 902FAD
Nucleotide binding464 – 4696FAD

Sites

Binding site891FAD; via amide nitrogen
Binding site1081Substrate
Binding site2791FAD; via amide nitrogen and carbonyl oxygen
Binding site3901Substrate
Binding site4751FAD; via amide nitrogen
Binding site4821Substrate; via carbonyl oxygen

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Ref.5
Glycosylation3791N-linked (GlcNAc...) Ref.5
Disulfide bond28 ↔ 191 Ref.5
Disulfide bond349 ↔ 430 Ref.5

Experimental info

Sequence conflict281C → E AA sequence Ref.2
Sequence conflict331D → N AA sequence Ref.2

Secondary structure

1 ................................................................................................ 516
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P81382-1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 5F9435718B3A3BDE

FASTA51658,221
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFDLRLNEF SQENDNAWYF IKNIRKKVGE VKKDPGLLKY PVKPSEAGKS AGQLYEESLG 

       190        200        210        220        230        240 
KVVEELKRTN CSYILNKYDT YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET 

       310        320        330        340        350        360 
PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT TKFWEDDGIH 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ ALDFKDCADI VFNDLSLIHQ 

       430        440        450        460        470        480 
LPKKDIQSFC YPSVIQKWSL DKYAMGGITT FTPYQFQHFS DPLTASQGRI YFAGEYTAQA 

       490        500        510 
HGWIDSTIKS GLRAARDVNL ASENPSGIHL SNDNEL

« Hide

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References

[1]"L-amino-acid oxidase from Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzyme."
Macheroux P., Seth O., Bollschweiler C., Schwarz M., Kurfuerst M., Au L.-C., Ghisla S.
Eur. J. Biochem. 268:1679-1686(2001) [PubMed: 11248687] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-33.
Tissue: Venom and Venom gland.
[2]"Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
Ponnudurai G., Chung M.C.M., Tan N.-H.
Arch. Biochem. Biophys. 313:373-378(1994) [PubMed: 8080286] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-38, SUBUNIT.
Tissue: Venom.
[3]"Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma."
Kommoju P.R., Macheroux P., Ghisla S.
Protein Expr. Purif. 52:89-95(2007) [PubMed: 17127077] [Abstract]
Cited for: EXPRESSION OF ACTIVE RECOMBINANT LAAO.
[4]"L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria."
Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.
Toxicon 48:227-237(2006) [PubMed: 16828829] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]"The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site."
Pawelek P.D., Cheah J., Coulombe R., Macheroux P., Ghisla S., Vrielink A.
EMBO J. 19:4204-4215(2000) [PubMed: 10944103] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379.
Tissue: Venom.
[6]"Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism."
Moustafa I.M., Foster S., Lyubimov A.Y., Vrielink A.
J. Mol. Biol. 364:991-1002(2006) [PubMed: 17046020] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF LAAO IN COMPLEX WITH THE SUBSTRATE L-PHE.
Tissue: Venom.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ271725 mRNA. Translation: CAB71136.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8RX-ray2.00A/B/C/D19-516[»]
1F8SX-ray2.00A/B/C/D/E/F/G/H19-516[»]
2IIDX-ray1.80A/B/C/D19-516[»]
ModBaseSearch...

PTM databases

GlycoSuiteDBP81382.

Phylogenomic databases

HOVERGENP81382.

Enzyme and pathway databases

BRENDA1.4.3.2. 18614.

Family and domain databases

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

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Entry information

Entry nameOXLA_AGKRH
AccessionPrimary (citable) accession number: P81382
Secondary accession number(s): Q9I849
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2002
Last modified: November 24, 2009
This is version 67 of the entry and version 2 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

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