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B5U6Y8

- OXLA_ECHOC

UniProt

B5U6Y8 - OXLA_ECHOC

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Echis ocellatus (Ocellated saw-scaled viper)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 16 (01 Oct 2014)
      Sequence version 1 (04 Nov 2008)
      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. Its effect on platelets is controversial, since it either induces aggregation or inhibits 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 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
    OrganismiEchis ocellatus (Ocellated saw-scaled viper)
    Taxonomic identifieri99586 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

    Subcellular locationi

    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 – 504486L-amino-acid oxidasePRO_0000412602Add
    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.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

    ProteinModelPortaliB5U6Y8.
    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.

    B5U6Y8-1 [UniParc]FASTAAdd to Basket

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    MNIFFMFSLL FLATLGSCAD DKNPLEECFR EADYEEFLEI AKNGLKKTSN    50
    PKDIVVVGAG MSGLSAAYVL AGAGHKVTVL EASQLVGGRV RTHRNAKEGW 100
    YANLGPMRIP EKHRIVREYI RKFGLELNEF VQETDNGWYF VKNIRKRVGE 150
    VKKDPGLLKY PVKPSEAGKS AGQLYQEALG KAVEELKRTN CSYMLNKYDT 200
    YSTKEYLIKE GNLSTGAVDM IGDLMNEDSG YYVSFVESMK HDDIFAYEKR 250
    FDEIVGGMDQ LPTSMYRAIE KSVLFKARVT KIQQNAEKVR VTYQTAAKTL 300
    SDVTADYVIV CTTSRAARRI NFKPPLPPKK AHALRSVHYR SATKIFLTCT 350
    KKFWEDDGIQ GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDSNFFL 400
    SLTLNECADI VFSDLSSIHQ LPKNDIQKFC NPSVIQKWSL DRYAMGAITT 450
    FTPYQFQDYS KALTAPAGRV YFAGEYTANA HGWIDSTIKS GLTAARDVNQ 500
    ASEL 504
    Length:504
    Mass (Da):56,523
    Last modified:November 4, 2008 - v1
    Checksum:i602E5B4A9FCEE797
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM177950 mRNA. Translation: CAQ72894.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM177950 mRNA. Translation: CAQ72894.1 .

    3D structure databases

    ProteinModelPortali B5U6Y8.
    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. "Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus."
      Wagstaff S.C., Sanz L., Juarez P., Harrison R.A., Calvete J.J.
      J. Proteomics 71:609-623(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom and Venom gland.

    Entry informationi

    Entry nameiOXLA_ECHOC
    AccessioniPrimary (citable) accession number: B5U6Y8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 16 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3