Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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, 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). Inhibits growth of B.subtilis strain ATCC 6633 (MIC=32 µM), E.faecalis strain ATCC 12953 (MIC=32 µM), S.aureus strain ATCC 29213 (MIC=32 µM), S.pyogenes strain ATCC 19615 (MIC=8 µM), E.coli strain ATCC 8739 (MIC=4 µM), K.pneumoniae strain ATCC 13885 (MIC=2 µM), P.mirabilis strain ATCC 25933 (MIC=2 µM), P.aeruginosa strain ATCC 15442 (MIC=8 µM) and S.typhimurium strain ATCC 14028 (MIC=8 µM).By similarity1 Publication

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

FADBy 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
Complete GO annotation...

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 oxidase1 Publication (EC:1.4.3.21 Publication)
Short name:
Bm-LAO1 Publication
Short name:
LAAOBy similarity
Short name:
LAOBy similarity
OrganismiBothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis)
Taxonomic identifieri1171125 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›31›31L-amino-acid oxidasePRO_0000417918Add
BLAST

Post-translational modificationi

N-glycosylated.By similarity

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Homodimer; non-covalently linked.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.Sequence Analysis

Sequencei

Sequence statusi: Fragments.

B3EWI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
IKFEPPLPPK KAHKKFWEDD GIYYPPNHNF P
Length:31
Mass (Da):3,751
Last modified:June 13, 2012 - v1
Checksum:i778F60FA5F08EB99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 111 Publication
Non-adjacent residuesi13 – 1421 Publication
Non-adjacent residuesi21 – 2221 Publication
Non-terminal residuei31 – 3111 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom."
    Okubo B.M., Silva O.N., Migliolo L., Gomes D.G., Porto W.F., Batista C.L., Ramos C.S., Holanda H.H., Dias S.C., Franco O.L., Moreno S.E.
    PLoS ONE 7:E33639-E33639(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Tissue: Venom1 Publication.

Entry informationi

Entry nameiOXLA_BOTMT
AccessioniPrimary (citable) accession number: B3EWI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: June 13, 2012
Last modified: January 7, 2015
This is version 12 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.