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
Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
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 apoptosis, and inhibition of agonist- and shear stress-induced platelet aggregation (SIPA). 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. This protein may also induce hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities.2 Publications

Catalytic activityi

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

Cofactori

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, Platelet aggregation inhibiting toxin, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.2. 194.

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
Short name:
M-LAO
OrganismiGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Taxonomic identifieri242054 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_500004991619 – 504L-amino-acid oxidaseAdd BLAST486

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ90W54.
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.
IPR001613. Flavin_amine_oxidase.
[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.

Q90W54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN
60 70 80 90 100
PKHVVIVGAG MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEGW
110 120 130 140 150
YANLGPMRLP EKHRIVREYI RKFGLQLNEF SQENDNAWYF IKNIRKRVGE
160 170 180 190 200
VKKDPGVLKY PVKPSEEGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT
210 220 230 240 250
YSTKEYLLKE GNLSPGAVDM IGDLMNEDSG YYVSFPESLR HDDIFAYEKR
260 270 280 290 300
FDEIVGGMDK LPTSMYRAIE EKVHLNAQVI KIQKNAEKVT VVYQTPAKEM
310 320 330 340 350
ASVTADYVIV CTTSRATRRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT
360 370 380 390 400
KKFWEDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDFKDCADI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT
460 470 480 490 500
FTPYQFQHFS EPLTASVDRI YFAGEHTAEA HGWIDSTIKS GLRAARDVNR

ASEQ
Length:504
Mass (Da):57,092
Last modified:December 1, 2001 - v1
Checksum:i17F57B46E646F12A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072392 mRNA. Translation: BAB69450.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072392 mRNA. Translation: BAB69450.1.

3D structure databases

ProteinModelPortaliQ90W54.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005729.

Enzyme and pathway databases

BRENDAi1.4.3.2. 194.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiOXLA_GLOBL
AccessioniPrimary (citable) accession number: Q90W54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: October 5, 2016
This is version 68 of the entry and version 1 of the sequence. [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.