Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A8QL51

- OXLA_BUNMU

UniProt

A8QL51 - OXLA_BUNMU

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bungarus multicinctus (Many-banded krait)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 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

    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:
    Bm-LAAO
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiBungarus multicinctus (Many-banded krait)
    Taxonomic identifieri8616 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

    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 – 517499L-amino-acid oxidasePRO_0000412600Add
    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

    Homodimer; non-covalently linked.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliA8QL51.
    SMRiA8QL51. 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.

    A8QL51-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFSIFSLV FLAAFGSCAD DRRSPLEECF READYEEFLE IARNGLKKTS    50
    NPKHVVVVGA GMAGLSAAYV LEKAGHRVTL LEASDRVGGR ANTYRDEKEG 100
    WYVNMGPMRL PERHRIVRTY IAKFGLKLNE FFQENENAWY FIRNIRKRVW 150
    EVKKDPGVFK YPVKPSEEGK SASQLYRESL KKIIEELKRT NCSYILDKYD 200
    SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL KNDDLFSYEK 250
    RFDEISGGFD QLPKSMHQDI AEMVHLNAQV TKIQHDAEKV RVAYQTPAKT 300
    LSYVTADYVI VCATSRAVRR ISFEPPLPSK KAHALRSIHY KSATKIFLTC 350
    TQKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YVLADDSDFF 400
    QALDIKTSAD IVINDLSLIH QLPKNEIQAL CYPSLIKKWS LDKYTMGALT 450
    SFTPYQFQDY SETVAAPVGR IYFAGEYTAR VHGWLDSTIK SGLTAARDVN 500
    RASQKPSRIH LISDNQL 517
    Length:517
    Mass (Da):58,811
    Last modified:January 15, 2008 - v1
    Checksum:iA9F28766C1B3AB97
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF080832 mRNA. Translation: ABN72539.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF080832 mRNA. Translation: ABN72539.1 .

    3D structure databases

    ProteinModelPortali A8QL51.
    SMRi A8QL51. Positions 23-505.
    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 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.

    Entry informationi

    Entry nameiOXLA_BUNMU
    AccessioniPrimary (citable) accession number: A8QL51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 29 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