Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B5U6Y8

- OXLA_ECHOC

UniProt

B5U6Y8 - OXLA_ECHOC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Echis ocellatus (Ocellated saw-scaled viper)
Status
Reviewed - Annotation score: 3 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. Its effect on platelets is controversial, since it either induces aggregation or inhibits 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FADBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Binding sitei241 – 2411SubstrateBy similarity
Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei390 – 3901SubstrateBy similarity
Binding sitei475 – 4751FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FADBy similarity
Nucleotide bindingi81 – 822FADBy similarity
Nucleotide bindingi105 – 1084FADBy similarity
Nucleotide bindingi482 – 4876FADBy similarity
Nucleotide bindingi482 – 4832SubstrateBy similarity

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
  3. hemolysis in other organism Source: UniProtKB-KW
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
OrganismiEchis ocellatus (Ocellated saw-scaled viper)
Taxonomic identifieri99586 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 504486L-amino-acid oxidasePRO_0000412602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 191By similarity
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi349 ↔ 430By similarity
Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis

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

ProteinModelPortaliB5U6Y8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B5U6Y8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIFFMFSLL FLATLGSCAD DKNPLEECFR EADYEEFLEI AKNGLKKTSN
60 70 80 90 100
PKDIVVVGAG MSGLSAAYVL AGAGHKVTVL EASQLVGGRV RTHRNAKEGW
110 120 130 140 150
YANLGPMRIP EKHRIVREYI RKFGLELNEF VQETDNGWYF VKNIRKRVGE
160 170 180 190 200
VKKDPGLLKY PVKPSEAGKS AGQLYQEALG KAVEELKRTN CSYMLNKYDT
210 220 230 240 250
YSTKEYLIKE GNLSTGAVDM IGDLMNEDSG YYVSFVESMK HDDIFAYEKR
260 270 280 290 300
FDEIVGGMDQ LPTSMYRAIE KSVLFKARVT KIQQNAEKVR VTYQTAAKTL
310 320 330 340 350
SDVTADYVIV CTTSRAARRI NFKPPLPPKK AHALRSVHYR SATKIFLTCT
360 370 380 390 400
KKFWEDDGIQ GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDSNFFL
410 420 430 440 450
SLTLNECADI VFSDLSSIHQ LPKNDIQKFC NPSVIQKWSL DRYAMGAITT
460 470 480 490 500
FTPYQFQDYS KALTAPAGRV YFAGEYTANA HGWIDSTIKS GLTAARDVNQ

ASEL
Length:504
Mass (Da):56,523
Last modified:November 4, 2008 - v1
Checksum:i602E5B4A9FCEE797
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM177950 mRNA. Translation: CAQ72894.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM177950 mRNA. Translation: CAQ72894.1 .

3D structure databases

ProteinModelPortali B5U6Y8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005729.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus."
    Wagstaff S.C., Sanz L., Juarez P., Harrison R.A., Calvete J.J.
    J. Proteomics 71:609-623(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom and Venom gland.

Entry informationi

Entry nameiOXLA_ECHOC
AccessioniPrimary (citable) accession number: B5U6Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: November 4, 2008
Last modified: November 26, 2014
This is version 18 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

External Data

Dasty 3