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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active against L-Lys, L-Arg, L-Ala and L-Asn), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as edema, inflammatory cell infiltration, cytotoxicity and apoptosis, as well as induction 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. This protein may also induce hemorrhage, hemolysis, and have antibacterial and antiparasitic activities.1 Publication

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

FADBy similarity

Kineticsi

  1. KM=28.28 mM for L-Ala1 Publication
  2. KM=18.75 mM for L-Arg1 Publication
  3. KM=0.04 mM for L-Asp1 Publication
  4. KM=19.07 mM for L-Asn1 Publication
  5. KM=5.88 mM for L-Gln1 Publication
  6. KM=1.44 mM for L-Glu1 Publication
  7. KM=4.84 mM for L-His1 Publication
  8. KM=1.64 mM for L-Ile1 Publication
  9. KM=60.69 mM for L-Leu1 Publication
  10. KM=21.49 mM for L-Lys1 Publication
  11. KM=15.03 mM for L-Met1 Publication
  12. KM=0.13 mM for L-Phe1 Publication
  13. KM=0.27 mM for L-Trp1 Publication
  14. KM=0.05 mM for L-Tyr1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901FADBy similarity
    Binding sitei109 – 1091SubstrateBy similarity
    Binding sitei280 – 2801FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei391 – 3911SubstrateBy similarity
    Binding sitei476 – 4761FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi62 – 632FADBy similarity
    Nucleotide bindingi82 – 832FADBy similarity
    Nucleotide bindingi106 – 1094FADBy similarity
    Nucleotide bindingi483 – 4886FADBy similarity
    Nucleotide bindingi483 – 4842SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation activating toxin, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BRENDAi1.4.3.2. 1026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    Bf-LAAO
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiBungarus fasciatus (Banded krait) (Pseudoboa fasciata)
    Taxonomic identifieri8613 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 517498L-amino-acid oxidasePRO_0000412599Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 192By similarity
    Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi350 ↔ 431By similarity
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliA8QL52.
    SMRiA8QL52. Positions 23-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A8QL52-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNVFSIFSLV FLAAFGSCAD DRRSALEECF READYEEFLE IARNGLKKTS
    60 70 80 90 100
    NPKHVVVVGA GMAGLSAAYV LAGAGHRVTL LEASDRVGGR VNTYRDEKEG
    110 120 130 140 150
    WYVNMGPMRL PERHRIVRTY IAKFGLKLNE FFQENENAWY FIRNIRKRVW
    160 170 180 190 200
    EVKKDPGVFK YPVKPSEEGK SASQLYRESL KKVIEELKRT NCSYILDKYD
    210 220 230 240 250
    TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL KNDDLFSYEK
    260 270 280 290 300
    RFDEISDGFD QLPKSMHQAI AEMVHLNAQV IKIQRDAEKV RVAYQTPAKT
    310 320 330 340 350
    LSYVTADYVI VCATSRAVRR ISFEPPLPPK KAHALRSIHY KSATKIFLTC
    360 370 380 390 400
    TRKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YVLADDSDFF
    410 420 430 440 450
    QALDIKTSAD IVINDLSLIH QLPKNEIQAL CYPSLIKKWS LDKYTMGALT
    460 470 480 490 500
    SFTPYQFQDY IETVAAPVGR IYFAGEYTAT VHGWLDSTIK SGLTAARNVN
    510
    RASQKPSRIH LINDNQL
    Length:517
    Mass (Da):58,764
    Last modified:January 15, 2008 - v1
    Checksum:iE869950FB941B11D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF080833 mRNA. Translation: ABN72540.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF080833 mRNA. Translation: ABN72540.1.

    3D structure databases

    ProteinModelPortaliA8QL52.
    SMRiA8QL52. Positions 23-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOVERGENiHBG005729.

    Enzyme and pathway databases

    BRENDAi1.4.3.2. 1026.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular characterization of L-amino acid oxidase from king cobra venom."
      Jin Y., Lee W.-H., Zeng L., Zhang Y.
      Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Venom gland.
    2. "Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom."
      Wei J.-F., Yang H.-W., Wei X.-L., Qiao L.-Y., Wang W.-Y., He S.-H.
      Toxicon 54:262-271(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-36, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_BUNFA
    AccessioniPrimary (citable) accession number: A8QL52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: January 15, 2008
    Last modified: April 1, 2015
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.