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B5AR80

- OXLA_BOTPA

UniProt

B5AR80 - OXLA_BOTPA

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly against L-Met, L-Leu, L-Phe and L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as antibacterial on both Gram-positive and Gram-negative bacteria and antiparasitic activities, as well as induction 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. This protein may also have activities in hemorrhage, hemolysis, edema, and apoptosis.1 Publication

    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, 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:
    Bp-LAAO
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiBothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis)
    Taxonomic identifieri1042543 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

    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 – 18182 PublicationsAdd
    BLAST
    Chaini19 – ›503›485L-amino-acid oxidasePRO_0000412598Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation.1 PublicationCurated

    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

    ProteinModelPortaliB5AR80.
    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.

    B5AR80-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFFMFSLL FLAALGSCAD DGNPLEECFR ETDYEEFLEI AKNGLSATSN    50
    PKHVVIVGAG MSGLSAAYVL ANAGHQVTVL EASKRAGGRV RTYRNDKEGW 100
    YANLGPMRLP EKHRIVREYI RKFGLQLNEF SQENENAWYF IKNIRKRVGE 150
    VNKDPGVLEY PVKPSEVGKS AGQLYEESLQ KAVEELRRTN CSYMLNKYDT 200
    YSTKEYLLKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR 250
    FDEIVGGMDK LPTSMYQAIQ EKVRLNVRVI KIQQDVKEVT VTYQTSAKET 300
    LSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT 350
    KKFWEDDGIH GGKSTTDLPS RFIYYPNHNF PSGVGVIIAY GIGDDANFFQ 400
    ALDFKDCGDI VINDLSLIHQ LPKEEIQAFC RPSMIQRWSL DKYAMGGITT 450
    FTPYQFQHFS EALTAPVDRI YFAGEYTAQA HGWIDSTIKS GLTAARDVNR 500
    ASE 503
    Length:503
    Mass (Da):56,799
    Last modified:September 23, 2008 - v1
    Checksum:i800568E8C2166CD0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei503 – 5031

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU870608 mRNA. Translation: ACG55578.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU870608 mRNA. Translation: ACG55578.1 .

    3D structure databases

    ProteinModelPortali B5AR80.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-68, FUNCTION, SUBUNIT, GLYCOSYLATION.
      Tissue: Venom and Venom gland.
    2. "Combined snake venomics and venom gland transcriptomic analysis of Bothropoides pauloensis."
      Rodrigues R.S., Boldrini-Franca J., Fonseca F.P., de la Torre P., Henrique-Silva F., Sanz L., Calvete J.J., Rodrigues V.M.
      J. Proteomics 75:2707-2720(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-34, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_BOTPA
    AccessioniPrimary (citable) accession number: B5AR80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 24 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

    Miscellaneous

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

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3