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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
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 sitei90FADBy similarity1
Binding sitei109SubstrateBy similarity1
Binding sitei280FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei391SubstrateBy similarity1
Binding sitei476FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi62 – 63FADBy similarity2
Nucleotide bindingi82 – 83FADBy similarity2
Nucleotide bindingi106 – 109FADBy similarity4
Nucleotide bindingi483 – 488FADBy similarity6
Nucleotide bindingi483 – 484SubstrateBy 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
OrganismiNotechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
Taxonomic identifieri70142 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaeNotechis

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_500014037919 – 517L-amino-acid oxidaseAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 192By similarity
Glycosylationi191N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi350 ↔ 431By similarity
Glycosylationi380N-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

ProteinModelPortaliQ4JHE2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q4JHE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALESCAD DRRRPLEECF QEADYEEFLE IARNGLNETS
60 70 80 90 100
NPKHVVVVGA GMAGLSAAYV LAGAGHNVTL LEASERVGGR VNTYRNETEG
110 120 130 140 150
WYVNLGPMRL PERHRIIREY IRKFGLKLNE FLQENENAWY FIRNIRKRVW
160 170 180 190 200
EVKKDPGVFK YPVEPSEEGK SASQLYRESL EKVIEELKRT NCSYILNKYD
210 220 230 240 250
TYSTKEYLIK EGNLSRGAVD MIGKLPNEDS SYYLSFIESL KSDDLFSYEK
260 270 280 290 300
RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEEV RVAYQTPAKT
310 320 330 340 350
LSYVTADYVI VCSTSRAARR IYFEPPLPPK KAHALRSIHY RSGTKIFLTC
360 370 380 390 400
TRKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSDVGVIVA YTLADDADFF
410 420 430 440 450
QALDIKTSAD IVINDLSLIH QLPKEEIQAL CYPSMIKKWS LDKYAMGAIT
460 470 480 490 500
SFTPYQFQDF IETVAAPVGR IYFAGEYTAR VHGWLDSTIK SGLTAARDVN
510
RASQKPSRRQ LSNDNEL
Length:517
Mass (Da):59,058
Last modified:August 2, 2005 - v1
Checksum:iE5A0DFF675FF34E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ088991 mRNA. Translation: AAY89681.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ088991 mRNA. Translation: AAY89681.1.

3D structure databases

ProteinModelPortaliQ4JHE2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiOXLA_NOTSC
AccessioniPrimary (citable) accession number: Q4JHE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: August 2, 2005
Last modified: October 5, 2016
This is version 60 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.