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Q6TGQ9

- OXLA_BOTJR

UniProt

Q6TGQ9 - OXLA_BOTJR

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops jararacussu (Jararacussu)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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, as well as regulation 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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031SubstrateBy similarity
    Binding sitei236 – 2361SubstrateBy similarity
    Binding sitei274 – 2741FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei385 – 3851SubstrateBy similarity
    Binding sitei470 – 4701FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi56 – 572FADBy similarity
    Nucleotide bindingi76 – 772FADBy similarity
    Nucleotide bindingi100 – 1034FADBy similarity
    Nucleotide bindingi477 – 4826FADBy similarity
    Nucleotide bindingi477 – 4782SubstrateBy 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

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, 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:
    BjussuLAAO-I
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiBothrops jararacussu (Jararacussu)
    Taxonomic identifieri8726 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1313By similarityAdd
    BLAST
    Chaini14 – ›497›484L-amino-acid oxidasePRO_0000273564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 186By similarity
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi344 ↔ 425By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.1 Publication

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.By similarity

    Structurei

    Secondary structure

    1
    497
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 3811
    Beta strandi48 – 514
    Helixi56 – 6712
    Beta strandi71 – 766
    Beta strandi78 – 814
    Beta strandi87 – 904
    Turni91 – 944
    Beta strandi95 – 984
    Helixi106 – 1083
    Helixi109 – 1168
    Turni117 – 1193
    Beta strandi122 – 1243
    Beta strandi133 – 1364
    Beta strandi139 – 1424
    Helixi143 – 1486
    Helixi151 – 1533
    Turni159 – 1635
    Helixi166 – 1727
    Turni173 – 1775
    Turni179 – 1846
    Helixi186 – 1949
    Beta strandi195 – 1973
    Helixi198 – 2036
    Turni204 – 2063
    Helixi210 – 21910
    Turni223 – 2275
    Helixi230 – 24011
    Beta strandi246 – 2494
    Helixi255 – 2639
    Helixi264 – 2674
    Beta strandi268 – 2714
    Beta strandi274 – 2796
    Beta strandi284 – 2896
    Beta strandi299 – 3057
    Helixi309 – 3135
    Beta strandi315 – 3195
    Helixi323 – 3319
    Beta strandi337 – 34610
    Helixi348 – 3503
    Turni351 – 3533
    Beta strandi356 – 3638
    Beta strandi366 – 3705
    Turni376 – 3783
    Beta strandi380 – 3878
    Helixi389 – 3924
    Turni393 – 3964
    Helixi399 – 41315
    Helixi418 – 4236
    Beta strandi425 – 4339
    Turni437 – 4393
    Beta strandi440 – 4445
    Helixi450 – 45910
    Beta strandi463 – 4675
    Turni470 – 4723
    Beta strandi473 – 4775
    Helixi480 – 4834
    Helixi488 – 4958

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E0VX-ray3.10A/B1-497[»]
    ProteinModelPortaliQ6TGQ9.
    SMRiQ6TGQ9. Positions 16-497.
    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: Fragment.

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

    Q6TGQ9-1 [UniParc]FASTAAdd to Basket

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    MNVFFMFSKP GKLADDRNPL EECFRETDYE EFLEIAKNGL STTSNPKRVV    50
    IVGAGMSGLS AAYVLANAGH QVTVLEASER AGGQVKTYRN EKEGWYANLG 100
    PMRLPEKHRI VREYIRKFGL QLNEFSQENE NAWYFIKNIR KRVGEVNKDP 150
    GVLDYPVKPS EVGKSAGQLY EESLQKAVEE LRRTNCSYML NKYDTYSTKE 200
    YLLKEGNLSP GAVDMIGDLL NEDSGYYVSF IESLKHDDIF AYEKRFDEIV 250
    GGMDKLPTSM YQAIQEKVHL NARVIKIQQD VKEVTVTYQT SEKETLSVTA 300
    DYVIVCTTSR AARRIKFEPP LPPKKAHALR SVHYRSGTKI FLTCTKKFWE 350
    DDGIHGGKST TDLPSRFIYY PNHNFPNGVG VIIAYGIGDD ANYFEALDFE 400
    DCGDIVINDL SLIHQLPKEE IQAICRPSMI QRWSLDKYAM GGITTFTPYQ 450
    FQHFSEALTA PVDRIYFAGE YTAQAHGWIA STIKSGPEGL DVNRASE 497
    Length:497
    Mass (Da):56,289
    Last modified:July 5, 2004 - v1
    Checksum:i51AFCB28038399A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei497 – 4971

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY398691 mRNA. Translation: AAR31182.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY398691 mRNA. Translation: AAR31182.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4E0V X-ray 3.10 A/B 1-497 [» ]
    ProteinModelPortali Q6TGQ9.
    SMRi Q6TGQ9. Positions 16-497.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005729.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00757. AMINEOXDASEF.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling."
      Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O., Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V., Soares A.M.
      Biochem. Biophys. Res. Commun. 355:302-306(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Venom and Venom gland.

    Entry informationi

    Entry nameiOXLA_BOTJR
    AccessioniPrimary (citable) accession number: Q6TGQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.1 Publication

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3