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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops atrox (Barba amarilla) (Fer-de-lance)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Met, followed by L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as apoptosis, cytotoxicity towards several cancer cell lines, induction of platelet aggregation, induction of moderate mouse paw edema, and antibacterial activities against both Gram-positive and Gram-negative bacteria. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 µg of enzyme). May also act in hemolysis, and antiparasitic activities. 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.2 Publications

Miscellaneous

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

Catalytic activityi

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

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70SubstrateBy similarity1
Binding sitei106FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi112 – 117FADBy similarity6

GO - Molecular functioni

  • L-amino-acid oxidase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • envenomation resulting in positive regulation of platelet aggregation in other organism Source: UniProtKB
  • hemolysis in other organism Source: UniProtKB-KW
  • modulation of apoptotic process in other organism Source: UniProtKB
  • regulation of platelet aggregation Source: UniProtKB

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation activating toxin, Toxin
Biological processApoptosis, Cytolysis, Hemolysis
LigandFAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
BatroxLAAO
Short name:
LAAO
Short name:
LAO
OrganismiBothrops atrox (Barba amarilla) (Fer-de-lance)
Taxonomic identifieri8725 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000390927‹1 – ›119L-amino-acid oxidaseAdd BLAST›119

Post-translational modificationi

Contains 2 disulfide bonds.By similarity
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Homodimer; non-covalently linked.By similarity

Structurei

3D structure databases

SMRiP0CC17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 113Substrate bindingBy similarity2

Sequence similaritiesi

Sequencei

Sequence statusi: Fragments.

P0CC17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADDRNPLEER KFDLQLNRFS QENENAWYFI KNRVGEVNKD PGVLEYPVKP
60 70 80 90 100
SEVGKSSAGQ LYEESLQKAH DDIFAYEKIK FEPPLPPKKF WEDDGIHGGK
110
IYFAGETAQA HGWIDSTIK
Length:119
Mass (Da):13,700
Last modified:January 19, 2010 - v1
Checksum:i9006A71038ED323D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-adjacent residuesi9 – 10Curated2
Non-adjacent residuesi32 – 33Curated2
Non-adjacent residuesi69 – 70Curated2
Non-adjacent residuesi78 – 79Curated2
Non-adjacent residuesi88 – 89Curated2
Non-adjacent residuesi100 – 101Curated2
Non-terminal residuei1191

Cross-referencesi

3D structure databases

SMRiP0CC17.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiOXLA_BOTAT
AccessioniPrimary (citable) accession number: P0CC17
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: January 19, 2010
Last modified: March 15, 2017
This is version 18 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.