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Q6WP39

- OXLA_TRIST

UniProt

Q6WP39 - OXLA_TRIST

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Status
Reviewed - Annotation score: 4 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
    Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication.

    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 sitei89 – 891FADBy similarity
    Binding sitei108 – 1081SubstrateBy similarity
    Binding sitei241 – 2411SubstrateBy similarity
    Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei390 – 3901SubstrateBy similarity
    Binding sitei475 – 4751FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 622FADBy similarity
    Nucleotide bindingi81 – 822FADBy similarity
    Nucleotide bindingi105 – 1084FADBy similarity
    Nucleotide bindingi482 – 4876FADBy similarity
    Nucleotide bindingi482 – 4832SubstrateBy 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:
    LAAO
    Short name:
    LAO
    Short name:
    TSV-LAO
    OrganismiTrimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
    Taxonomic identifieri39682 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeTrimeresurus

    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 – 1818By similarityAdd
    BLAST
    Chaini19 – 516498L-amino-acid oxidasePRO_0000273572Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 191By similarity
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi349 ↔ 430By similarity
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ6WP39.
    SMRiQ6WP39. Positions 21-503.
    ModBaseiSearch...
    MobiDBiSearch...

    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: Complete.

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

    Q6WP39-1 [UniParc]FASTAAdd to Basket

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    MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN    50
    PKHVVIVGAG MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW 100
    YANLGPMRLP EKHRIVREYI RKFNLQLNEF SQENDNAWHF VKNIRKTVGE 150
    VKKDPGVLKY PVKPSEEGKS AEQLYEESLR KVEKELKRTN CSYILNKYDT 200
    YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK HDDIFAYEKR 250
    FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT 300
    SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT 350
    KKFREDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ 400
    ALDLKDCGDI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT 450
    FTPYQFQHFS EALTSHVDRI YFAGEYTAHA HGWIDSSIKS GLTAARDVNR 500
    ASENPSGIHL SNDDEL 516
    Length:516
    Mass (Da):58,601
    Last modified:July 5, 2004 - v1
    Checksum:iFB5AC0BC171B9288
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161G → E in AAQ16182. 1 PublicationCurated
    Sequence conflicti53 – 531H → R in AAQ16182. 1 PublicationCurated
    Sequence conflicti73 – 731A → T in AAQ16182. 1 PublicationCurated
    Sequence conflicti181 – 1811K → E in AAQ16182. 1 PublicationCurated
    Sequence conflicti294 – 2941H → Q in AAQ16182. 1 PublicationCurated
    Sequence conflicti315 – 3151R → G in AAQ16182. 1 PublicationCurated
    Sequence conflicti354 – 3541R → W in AAQ16182. 1 PublicationCurated
    Sequence conflicti514 – 5141D → N in AAQ16182. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY277739 mRNA. Translation: AAQ56232.1.
    AY338966 mRNA. Translation: AAQ16182.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY277739 mRNA. Translation: AAQ56232.1 .
    AY338966 mRNA. Translation: AAQ16182.1 .

    3D structure databases

    ProteinModelPortali Q6WP39.
    SMRi Q6WP39. Positions 21-503.
    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 Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity."
      Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y.
      Biochem. Biophys. Res. Commun. 309:598-604(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom and Venom gland.
    2. "Purification, cloning and characterization of the L-amino acid oxidase in snake Trimeresurus stejnegeri."
      Wang J., Huang Q., Teng M., Niu L.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Venom gland.

    Entry informationi

    Entry nameiOXLA_TRIST
    AccessioniPrimary (citable) accession number: Q6WP39
    Secondary accession number(s): Q7T062
    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 programChordata Protein Annotation Program
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3