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A8QL58

- OXLA_NAJAT

UniProt

A8QL58 - OXLA_NAJAT

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Protein
L-amino-acid oxidase
Gene
N/A
Organism
Naja atra (Chinese cobra)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities By similarity. This protein induces platelet aggregation by both hydrogen peroxide production and binding to platelet membrane proteins (that would enhance the sensitivity of platelets to hydrogen peroxide). 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.1 Publication

Catalytic activityi

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

Cofactori

FAD By similarity.

Kineticsi

    Vmax=38.4 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901FAD By similarity
    Binding sitei109 – 1091Substrate By similarity
    Binding sitei280 – 2801FAD; via amide nitrogen and carbonyl oxygen By similarity
    Binding sitei389 – 3891Substrate By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi62 – 632FAD By similarity
    Nucleotide bindingi82 – 832FAD By similarity
    Nucleotide bindingi106 – 1094FAD By similarity

    GO - Molecular functioni

    1. L-amino-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW
    3. hemolysis in other organism Source: UniProtKB-KW
    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    LAAO
    Short name:
    LAO
    Short name:
    NA-LAAO
    OrganismiNaja atra (Chinese cobra)
    Taxonomic identifieri8656 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 Publication
    Add
    BLAST
    Chaini20 – ›449›430L-amino-acid oxidase
    PRO_0000412603Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 192 By similarity
    Glycosylationi191 – 1911N-linked (GlcNAc...) Reviewed prediction
    Disulfide bondi348 ↔ 429 By similarity
    Glycosylationi378 – 3781N-linked (GlcNAc...) Reviewed prediction

    Post-translational modificationi

    N-glycosylated By similarity.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked By similarity.

    Structurei

    3D structure databases

    ProteinModelPortaliA8QL58.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

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

    A8QL58-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVLFIFSLL FLAALESCAD DRRSPLEECF QQNDYEEILE IARNGLKKTS    50
    NPKHVVVVGA GMAGLSAAYV LAGAGHKVTL LEASERVGGR VITYHNDREG 100
    WYVNMGPMRL PERHRIVREY IRKFGLKLNE FFQENENAWY YINNIRKRVW 150
    EVKKDPSLLK YPVKPSEEGK SASQLYQEPL RKVIEELKRT NCSYILNKYD 200
    SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYHLSFMESL KSDALFSYEK 250
    RFDEIVGGFD QLPISMYQAI AEMVHLNARV IKIQYDAEKV RVTYQTPAKT 300
    FVTADYVIVC STSRAARRIY FEPPLPPKKA HALRSIHYRS ATKIFLTCSK 350
    KFWEADGIHG GKSTTDLPSR FIHYPNHNFT SGIGVIMAYV LADDSDFFQA 400
    LDTKTCADIV INDLSLIHDL PKREIQALCY PSIKKWNLDK YTMGSITSF 449
    Length:449
    Mass (Da):51,439
    Last modified:January 15, 2008 - v1
    Checksum:i905AD5DFB3D08362
    GO

    Non-terminal residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei449 – 4491

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF080839 mRNA. Translation: ABN72546.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF080839 mRNA. Translation: ABN72546.1 .

    3D structure databases

    ProteinModelPortali A8QL58.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005729.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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. "L-amino acid oxidase from Naja atra venom activates and binds to human platelets."
      Li R., Zhu S., Wu J., Wang W., Lu Q., Clemetson K.J.
      Acta Biochim. Biophys. Sin. 40:19-26(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-29, FUNCTION IN PLATELET AGGREGATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_NAJAT
    AccessioniPrimary (citable) accession number: A8QL58
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: January 15, 2008
    Last modified: February 19, 2014
    This is version 21 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

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