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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Crotalus atrox (Western diamondback rattlesnake)
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-Leu), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemolysis, edema, 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). In addition, this protein induces hemorrhage and apoptosis.By similarity1 Publication

Catalytic activityi

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

Cofactori

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

  • L-amino-acid oxidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemorrhagic toxin, 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
Alternative name(s):
Apoxin I
Apoxin-1
OrganismiCrotalus atrox (Western diamondback rattlesnake)
Taxonomic identifieri8730 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 183 PublicationsAdd BLAST18
ChainiPRO_000009987019 – 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. Glycosylation is needed for activity.1 Publication

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

ProteinModelPortaliP56742.
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.

P56742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN
60 70 80 90 100
PKRVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA
110 120 130 140 150
NLGPMRLPTK HRIVREYIKK FDLKLNEFSQ ENENAWYFIK NIRKRVREVK
160 170 180 190 200
NNPGLLEYPV KPSEEGKSAA QLYVESLRKV VKELKRTNCK 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 SGTKIFLTCK
360 370 380 390 400
KKFWEDDGIR GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDFKDCADI VINDLSLIHQ LPKEDIQTFC RPSMIQRWSL DKYAMGGITT
460 470 480 490 500
FTPYQFQHFS EALTAPFKRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR
510
ASENPSGIHL SNDNEF
Length:516
Mass (Da):58,767
Last modified:January 23, 2007 - v2
Checksum:i6CB90A49A0C015E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093248 mRNA. Translation: AAD45200.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093248 mRNA. Translation: AAD45200.1.

3D structure databases

ProteinModelPortaliP56742.
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_CROAT
AccessioniPrimary (citable) accession number: P56742
Secondary accession number(s): Q9PWC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 64 of the entry and version 2 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.