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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Status
Reviewed-Annotation score: Annotation score: 4 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, 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
Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication.

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 sitei108SubstrateBy similarity1
Binding sitei241SubstrateBy 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 bindingi105 – 108FADBy 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

Enzyme and pathway databases

BRENDAi1.4.3.2. 7401.

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
Short name:
TSV-LAO
OrganismiTrimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Taxonomic identifieri39682 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeTrimeresurus

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_000027357219 – 516L-amino-acid oxidaseAdd BLAST498

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 191By similarity
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi349 ↔ 430By similarity
Glycosylationi379N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ6WP39.
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.

Q6WP39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN
60 70 80 90 100
PKHVVIVGAG MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW
110 120 130 140 150
YANLGPMRLP EKHRIVREYI RKFNLQLNEF SQENDNAWHF VKNIRKTVGE
160 170 180 190 200
VKKDPGVLKY PVKPSEEGKS AEQLYEESLR KVEKELKRTN CSYILNKYDT
210 220 230 240 250
YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK HDDIFAYEKR
260 270 280 290 300
FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT
310 320 330 340 350
SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT
360 370 380 390 400
KKFREDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDLKDCGDI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT
460 470 480 490 500
FTPYQFQHFS EALTSHVDRI YFAGEYTAHA HGWIDSSIKS GLTAARDVNR
510
ASENPSGIHL SNDDEL
Length:516
Mass (Da):58,601
Last modified:July 5, 2004 - v1
Checksum:iFB5AC0BC171B9288
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16G → E in AAQ16182 (Ref. 2) Curated1
Sequence conflicti53H → R in AAQ16182 (Ref. 2) Curated1
Sequence conflicti73A → T in AAQ16182 (Ref. 2) Curated1
Sequence conflicti181K → E in AAQ16182 (Ref. 2) Curated1
Sequence conflicti294H → Q in AAQ16182 (Ref. 2) Curated1
Sequence conflicti315R → G in AAQ16182 (Ref. 2) Curated1
Sequence conflicti354R → W in AAQ16182 (Ref. 2) Curated1
Sequence conflicti514D → N in AAQ16182 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY277739 mRNA. Translation: AAQ56232.1.
AY338966 mRNA. Translation: AAQ16182.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY277739 mRNA. Translation: AAQ56232.1.
AY338966 mRNA. Translation: AAQ16182.1.

3D structure databases

ProteinModelPortaliQ6WP39.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005729.

Enzyme and pathway databases

BRENDAi1.4.3.2. 7401.

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_TRIST
AccessioniPrimary (citable) accession number: Q6WP39
Secondary accession number(s): Q7T062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: October 5, 2016
This is version 59 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.