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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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, 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

FADBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89FADBy similarity1
Binding sitei106SubstrateBy similarity1
Binding sitei239SubstrateBy similarity1
Binding sitei279FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei390SubstrateBy similarity1
Binding sitei475FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi61 – 62FADBy similarity2
Nucleotide bindingi81 – 82FADBy similarity2
Nucleotide bindingi103 – 106FADBy similarity4
Nucleotide bindingi482 – 487FADBy similarity6
Nucleotide bindingi482 – 483SubstrateBy similarity2

GO - Molecular functioni

GO - Biological processi

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 oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
OrganismiSistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
Taxonomic identifieri8762 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeSistrurus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000041260519 – 516L-amino-acid oxidaseAdd BLAST498

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 189By similarity
Disulfide bondi349 ↔ 430By similarity
Glycosylationi379N-linked (GlcNAc...)Sequence analysis1

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

ProteinModelPortaliB0VXW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B0VXW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLTATSN
60 70 80 90 100
PKRVVIVGAG MSGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKEDWYA
110 120 130 140 150
NLGPMRLPTK HRIVREYIKK FGLELNEFFQ ENDNAWYFIK NIRKRVQEVK
160 170 180 190 200
NNPGLLKYPV KPSETGKSAG QLYEESLRKV VEELRSTNCK YILDKYDTYS
210 220 230 240 250
TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD
260 270 280 290 300
EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM
310 320 330 340 350
SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT
360 370 380 390 400
KKFWEDEGIH GGKSTTDLPS RSIYYPNHNF TSGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDFKDCADI VINDLSLIHQ LPKEDIQTFC HPSKIQRWSL DRYAMGGITT
460 470 480 490 500
FTPYQFQHFS EALTAPFNRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR
510
ASENPSGIHL SNDNEF
Length:516
Mass (Da):58,569
Last modified:April 8, 2008 - v1
Checksum:iBABA9844650EB381
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ464267 mRNA. Translation: ABG26996.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ464267 mRNA. Translation: ABG26996.1.

3D structure databases

ProteinModelPortaliB0VXW0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiOXLA_SISCA
AccessioniPrimary (citable) accession number: B0VXW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: April 8, 2008
Last modified: October 5, 2016
This is version 26 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

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.