SubmitCancel

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.

Catalytic activityi

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

Cofactori

FAD By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD By similarity
Binding sitei108 – 1081Substrate By similarity
Binding sitei241 – 2411Substrate By similarity
Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei390 – 3901Substrate By similarity
Binding sitei475 – 4751FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FAD By similarity
Nucleotide bindingi81 – 822FAD By similarity
Nucleotide bindingi105 – 1084FAD By similarity
Nucleotide bindingi482 – 4876FAD By similarity
Nucleotide bindingi482 – 4832Substrate By 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-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

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

MNIFFMFSLL FLATLGSCAD DKNPLEECFR EADYEEFLEI AKNGLKKTSN    50
PKDIVVVGAG MSGLSAAYVL AGAGHKVTVL EASQLVGGRV RTHRNAKEGW 100
YANLGPMRIP EKHRIVREYI RKFGLELNEF VQETDNGWYF VKNIRKRVGE 150
VKKDPGLLKY PVKPSEAGKS AGQLYQEALG KAVEELKRTN CSYMLNKYDT 200
YSTKEYLIKE GNLSTGAVDM IGDLMNEDSG YYVSFVESMK HDDIFAYEKR 250
FDEIVGGMDQ LPTSMYRAIE KSVLFKARVT KIQQNAEKVR VTYQTAAKTL 300
SDVTADYVIV CTTSRAARRI NFKPPLPPKK AHALRSVHYR SATKIFLTCT 350
KKFWEDDGIQ GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDSNFFL 400
SLTLNECADI VFSDLSSIHQ LPKNDIQKFC NPSVIQKWSL DRYAMGAITT 450
FTPYQFQDYS KALTAPAGRV YFAGEYTANA HGWIDSTIKS GLTAARDVNQ 500
ASEL 504
Length:504
Mass (Da):56,523
Last modified:November 4, 2008 - v1
Checksum:i602E5B4A9FCEE797
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM177950 mRNA. Translation: CAQ72894.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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: February 19, 2014
This is version 15 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

Similar proteinsi