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O93364

- OXLA_CROAD

UniProt

O93364 - OXLA_CROAD

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Crotalus adamanteus (Eastern diamondback rattlesnake)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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 + H2O2.1 Publication

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891FADBy similarity
    Binding sitei106 – 1061SubstrateBy similarity
    Binding sitei239 – 2391SubstrateBy 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 bindingi103 – 1064FADBy 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
    Alternative name(s):
    Apoxin I
    Apoxin-1
    OrganismiCrotalus adamanteus (Eastern diamondback rattlesnake)
    Taxonomic identifieri8729 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

    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 – 18181 PublicationAdd
    BLAST
    Chaini19 – 516498L-amino-acid oxidasePRO_0000001706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 189By similarity
    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

    ProteinModelPortaliO93364.
    SMRiO93364. 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.

    O93364-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN    50
    PKRVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA 100
    NLGPMRLPTK HRIVREYIKK FDLKLNEFSQ ENENAWYFIK NIRKRVREVK 150
    NNPGLLEYPV KPSEEGKSAA QLYVESLRKV VEELRSTNCK YILDKYDTYS 200
    TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD 250
    EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 300
    SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT 350
    KKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ 400
    ALDFKDCADI VINDLSLIHE LPKEDIQTFC HPSMIQRWSL DKYAMGGITT 450
    FTPYQFQHFS EALTAPFKRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR 500
    ASENPSGIHL SNDNEF 516
    Length:516
    Mass (Da):58,662
    Last modified:November 1, 1998 - v1
    Checksum:iFDFAA77A49FDA05A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071564 mRNA. Translation: AAC32267.1.
    PIRiJE0266.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071564 mRNA. Translation: AAC32267.1 .
    PIRi JE0266.

    3D structure databases

    ProteinModelPortali O93364.
    SMRi O93364. 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. "Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein."
      Raibekas A.A., Massey V.
      Biochem. Biophys. Res. Commun. 248:476-478(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-44 AND 106-130.
      Tissue: Venom and Venom gland.
    2. "On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase."
      Massey V., Curti B.
      J. Biol. Chem. 242:1259-1264(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_CROAD
    AccessioniPrimary (citable) accession number: O93364
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 79 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

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3