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Q6TGQ9

- OXLA_BOTJR

UniProt

Q6TGQ9 - OXLA_BOTJR

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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops jararacussu (Jararacussu)
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. 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 sitei103 – 1031SubstrateBy similarity
Binding sitei236 – 2361SubstrateBy similarity
Binding sitei274 – 2741FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei385 – 3851SubstrateBy similarity
Binding sitei470 – 4701FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 572FADBy similarity
Nucleotide bindingi76 – 772FADBy similarity
Nucleotide bindingi100 – 1034FADBy similarity
Nucleotide bindingi477 – 4826FADBy similarity
Nucleotide bindingi477 – 4782SubstrateBy 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:
BjussuLAAO-I
Short name:
LAAO
Short name:
LAO
OrganismiBothrops jararacussu (Jararacussu)
Taxonomic identifieri8726 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

Secreted By similarity

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 – 1313By similarityAdd
BLAST
Chaini14 – ›497›484L-amino-acid oxidasePRO_0000273564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 186By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi344 ↔ 425By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Homodimer; non-covalently linked.By similarity

Structurei

Secondary structure

1
497
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3811
Beta strandi48 – 514
Helixi56 – 6712
Beta strandi71 – 766
Beta strandi78 – 814
Beta strandi87 – 904
Turni91 – 944
Beta strandi95 – 984
Helixi106 – 1083
Helixi109 – 1168
Turni117 – 1193
Beta strandi122 – 1243
Beta strandi133 – 1364
Beta strandi139 – 1424
Helixi143 – 1486
Helixi151 – 1533
Turni159 – 1635
Helixi166 – 1727
Turni173 – 1775
Turni179 – 1846
Helixi186 – 1949
Beta strandi195 – 1973
Helixi198 – 2036
Turni204 – 2063
Helixi210 – 21910
Turni223 – 2275
Helixi230 – 24011
Beta strandi246 – 2494
Helixi255 – 2639
Helixi264 – 2674
Beta strandi268 – 2714
Beta strandi274 – 2796
Beta strandi284 – 2896
Beta strandi299 – 3057
Helixi309 – 3135
Beta strandi315 – 3195
Helixi323 – 3319
Beta strandi337 – 34610
Helixi348 – 3503
Turni351 – 3533
Beta strandi356 – 3638
Beta strandi366 – 3705
Turni376 – 3783
Beta strandi380 – 3878
Helixi389 – 3924
Turni393 – 3964
Helixi399 – 41315
Helixi418 – 4236
Beta strandi425 – 4339
Turni437 – 4393
Beta strandi440 – 4445
Helixi450 – 45910
Beta strandi463 – 4675
Turni470 – 4723
Beta strandi473 – 4775
Helixi480 – 4834
Helixi488 – 4958

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E0VX-ray3.10A/B1-497[»]
ProteinModelPortaliQ6TGQ9.
SMRiQ6TGQ9. Positions 16-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Fragment.

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

Q6TGQ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVFFMFSKP GKLADDRNPL EECFRETDYE EFLEIAKNGL STTSNPKRVV
60 70 80 90 100
IVGAGMSGLS AAYVLANAGH QVTVLEASER AGGQVKTYRN EKEGWYANLG
110 120 130 140 150
PMRLPEKHRI VREYIRKFGL QLNEFSQENE NAWYFIKNIR KRVGEVNKDP
160 170 180 190 200
GVLDYPVKPS EVGKSAGQLY EESLQKAVEE LRRTNCSYML NKYDTYSTKE
210 220 230 240 250
YLLKEGNLSP GAVDMIGDLL NEDSGYYVSF IESLKHDDIF AYEKRFDEIV
260 270 280 290 300
GGMDKLPTSM YQAIQEKVHL NARVIKIQQD VKEVTVTYQT SEKETLSVTA
310 320 330 340 350
DYVIVCTTSR AARRIKFEPP LPPKKAHALR SVHYRSGTKI FLTCTKKFWE
360 370 380 390 400
DDGIHGGKST TDLPSRFIYY PNHNFPNGVG VIIAYGIGDD ANYFEALDFE
410 420 430 440 450
DCGDIVINDL SLIHQLPKEE IQAICRPSMI QRWSLDKYAM GGITTFTPYQ
460 470 480 490
FQHFSEALTA PVDRIYFAGE YTAQAHGWIA STIKSGPEGL DVNRASE
Length:497
Mass (Da):56,289
Last modified:July 5, 2004 - v1
Checksum:i51AFCB28038399A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei497 – 4971

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY398691 mRNA. Translation: AAR31182.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY398691 mRNA. Translation: AAR31182.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4E0V X-ray 3.10 A/B 1-497 [» ]
ProteinModelPortali Q6TGQ9.
SMRi Q6TGQ9. Positions 16-497.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005729.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00757. AMINEOXDASEF.
ProtoNeti Search...

Publicationsi

  1. "Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling."
    Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O., Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V., Soares A.M.
    Biochem. Biophys. Res. Commun. 355:302-306(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom and Venom gland.

Entry informationi

Entry nameiOXLA_BOTJR
AccessioniPrimary (citable) accession number: Q6TGQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 52 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

Miscellaneous

Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3