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B0VXW0

- OXLA_SISCA

UniProt

B0VXW0 - OXLA_SISCA

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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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

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 – 891FADBy similarity
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei239 – 2391SubstrateBy 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 bindingi103 – 1064FADBy 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
OrganismiSistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
Taxonomic identifieri8762 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeSistrurus

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 – 516498L-amino-acid oxidasePRO_0000412605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 189By similarity
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

ProteinModelPortaliB0VXW0.
SMRiB0VXW0. Positions 21-503.
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.

B0VXW0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLTATSN
60 70 80 90 100
PKRVVIVGAG MSGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKEDWYA
110 120 130 140 150
NLGPMRLPTK HRIVREYIKK FGLELNEFFQ ENDNAWYFIK NIRKRVQEVK
160 170 180 190 200
NNPGLLKYPV KPSETGKSAG QLYEESLRKV VEELRSTNCK 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 SGTKIFLTCT
360 370 380 390 400
KKFWEDEGIH GGKSTTDLPS RSIYYPNHNF TSGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDFKDCADI VINDLSLIHQ LPKEDIQTFC HPSKIQRWSL DRYAMGGITT
460 470 480 490 500
FTPYQFQHFS EALTAPFNRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR
510
ASENPSGIHL SNDNEF
Length:516
Mass (Da):58,569
Last modified:April 8, 2008 - v1
Checksum:iBABA9844650EB381
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ464267 mRNA. Translation: ABG26996.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ464267 mRNA. Translation: ABG26996.1 .

3D structure databases

ProteinModelPortali B0VXW0.
SMRi B0VXW0. Positions 21-503.
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. "The venom gland transcriptome of the Desert Massasauga rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (Superfamily Colubroidea)."
    Pahari S., Mackessy S.P., Kini R.M.
    BMC Mol. Biol. 8:115-115(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.

Entry informationi

Entry nameiOXLA_SISCA
AccessioniPrimary (citable) accession number: B0VXW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: April 8, 2008
Last modified: October 29, 2014
This is version 20 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3