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P0DI84

- OXLA_VIPAA

UniProt

P0DI84 - OXLA_VIPAA

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Vipera ammodytes ammodytes (Western sand viper)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 14 (01 Oct 2014)
      Sequence version 1 (21 Sep 2011)
      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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691FAD1 Publication
    Metal bindingi73 – 731Zinc
    Binding sitei88 – 881SubstrateBy similarity
    Binding sitei221 – 2211SubstrateBy similarity
    Binding sitei259 – 2591FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Metal bindingi277 – 2771Zinc
    Binding sitei370 – 3701SubstrateBy similarity
    Binding sitei455 – 4551FAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi41 – 422FAD1 Publication
    Nucleotide bindingi61 – 622FAD1 Publication
    Nucleotide bindingi85 – 884FAD1 Publication
    Nucleotide bindingi462 – 4676FAD1 Publication
    Nucleotide bindingi462 – 4632SubstrateBy similarity
    Nucleotide bindingi464 – 4674FAD1 Publication

    GO - Molecular functioni

    1. L-amino-acid oxidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    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, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    LAAO
    Short name:
    LAO
    Short name:
    VAA-LAAO I
    OrganismiVipera ammodytes ammodytes (Western sand viper)
    Taxonomic identifieri8705 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

    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
    Chaini1 – 484484L-amino-acid oxidasePRO_0000412591Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi8 ↔ 1711 Publication
    Glycosylationi170 – 1701N-linked (GlcNAc...)1 Publication
    Disulfide bondi329 ↔ 4101 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.1 Publication

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94
    Helixi14 – 2310
    Beta strandi33 – 375
    Helixi41 – 5212
    Beta strandi56 – 605
    Beta strandi62 – 676
    Beta strandi72 – 754
    Turni76 – 794
    Beta strandi80 – 856
    Helixi94 – 1029
    Beta strandi107 – 1104
    Beta strandi117 – 1215
    Beta strandi124 – 1274
    Helixi128 – 1336
    Helixi135 – 1384
    Helixi144 – 1463
    Helixi151 – 1588
    Helixi160 – 1667
    Helixi171 – 1777
    Helixi178 – 1803
    Helixi183 – 1897
    Helixi195 – 20410
    Helixi208 – 2103
    Helixi215 – 22511
    Beta strandi231 – 2344
    Helixi240 – 2489
    Helixi249 – 2524
    Beta strandi253 – 2564
    Beta strandi258 – 2647
    Beta strandi269 – 2746
    Beta strandi276 – 2783
    Beta strandi281 – 29010
    Helixi294 – 2974
    Beta strandi300 – 3045
    Helixi308 – 3169
    Beta strandi322 – 33110
    Helixi333 – 3375
    Beta strandi341 – 3488
    Beta strandi352 – 3543
    Beta strandi365 – 3728
    Helixi373 – 3808
    Helixi384 – 39916
    Helixi403 – 4097
    Beta strandi410 – 4178
    Helixi418 – 4203
    Turni422 – 4243
    Beta strandi425 – 4295
    Helixi435 – 44410
    Beta strandi450 – 4523
    Helixi455 – 4573
    Beta strandi458 – 4625
    Helixi464 – 48118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KVEX-ray2.57A/B/C/D1-484[»]
    ProteinModelPortaliP0DI84.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0DI84.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.

    Sequencei

    Sequence statusi: Complete.

    P0DI84-1 [UniParc]FASTAAdd to Basket

    « Hide

    DRNPLEECFR ETDYEEFLEI ARNGLKKTSN PKHVVVVGAG MSGLSAAYVL    50
    AGAGHKVTVL EASERAGGRV RTHRNSKEGW YANLGPMRIP EKHRIVREYI 100
    RKFGLNLNEF SQENDNAWYF IKNIRKRVGE VNKDPGLLKY PVKPSEEGKS 150
    AGQLYEESLG SAVKDLKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM 200
    IGDLLNEDSG YYVSFIESLK HDDIFAYEKR FDEIVGGMDQ LPTSMYRAIE 250
    EKVKFNARVI KIQQNANQVT VTYQTPEKDT SSNTADYVIV CTTSRAARRI 300
    QFEPPLPPKK QHALRSVHYR SGTKIFLTCS SKFWEDDGIH GGKSTTDLPS 350
    RFIYYPNHNF STGVGVIIAY GIGDDANFFQ ALKFKDCADI VFNDLSLIHQ 400
    LPKEEIQSFC YPSMIQKWSL DKYAMGAITT FTPYQFQRFS EALTAPQGRI 450
    FFAGEYTAEA HGWIDSTIKS GLTAARDVNR ASEQ 484
    Length:484
    Mass (Da):54,748
    Last modified:September 21, 2011 - v1
    Checksum:iFF2BBFB0EB5D1C47
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KVE X-ray 2.57 A/B/C/D 1-484 [» ]
    ProteinModelPortali P0DI84.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0DI84.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00757. AMINEOXDASEF.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom."
      Georgieva D., Kardas A., Buck F., Perbandt M., Betzel C.
      Acta Crystallogr. F 64:918-921(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION.
      Tissue: Venom.
    2. "Comparative analysis of the venom proteomes of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis."
      Georgieva D., Risch M., Kardas A., Buck F., von Bergen M., Betzel C.
      J. Proteome Res. 7:866-886(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom.
    3. "The structure of a native L-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions."
      Georgieva D., Murakami M., Perband M., Arni R., Betzel C.
      Mol. Biosyst. 7:379-384(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH FAD AND ZINC IONS, COFACTOR, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-170.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_VIPAA
    AccessioniPrimary (citable) accession number: P0DI84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 14 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

    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