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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops jararacussu (Jararacussu)
Status
Reviewed-Annotation score: 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

FADBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei103SubstrateBy similarity1
Binding sitei236SubstrateBy similarity1
Binding sitei274FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei385SubstrateBy similarity1
Binding sitei470FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 57FADBy similarity2
Nucleotide bindingi76 – 77FADBy similarity2
Nucleotide bindingi100 – 103FADBy similarity4
Nucleotide bindingi477 – 482FADBy similarity6
Nucleotide bindingi477 – 478SubstrateBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.2. 911.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 13By similarityAdd BLAST13
ChainiPRO_000027356414 – ›497L-amino-acid oxidaseAdd BLAST›484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi23 ↔ 186By similarity
Glycosylationi185N-linked (GlcNAc...)Sequence analysis1
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

1497
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 38Combined sources11
Beta strandi48 – 51Combined sources4
Helixi56 – 67Combined sources12
Beta strandi71 – 76Combined sources6
Beta strandi78 – 81Combined sources4
Beta strandi87 – 90Combined sources4
Turni91 – 94Combined sources4
Beta strandi95 – 98Combined sources4
Helixi106 – 108Combined sources3
Helixi109 – 116Combined sources8
Turni117 – 119Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi133 – 136Combined sources4
Beta strandi139 – 142Combined sources4
Helixi143 – 148Combined sources6
Helixi151 – 153Combined sources3
Turni159 – 163Combined sources5
Helixi166 – 172Combined sources7
Turni173 – 177Combined sources5
Turni179 – 184Combined sources6
Helixi186 – 194Combined sources9
Beta strandi195 – 197Combined sources3
Helixi198 – 203Combined sources6
Turni204 – 206Combined sources3
Helixi210 – 219Combined sources10
Turni223 – 227Combined sources5
Helixi230 – 240Combined sources11
Beta strandi246 – 249Combined sources4
Helixi255 – 263Combined sources9
Helixi264 – 267Combined sources4
Beta strandi268 – 271Combined sources4
Beta strandi274 – 279Combined sources6
Beta strandi284 – 289Combined sources6
Beta strandi299 – 305Combined sources7
Helixi309 – 313Combined sources5
Beta strandi315 – 319Combined sources5
Helixi323 – 331Combined sources9
Beta strandi337 – 346Combined sources10
Helixi348 – 350Combined sources3
Turni351 – 353Combined sources3
Beta strandi356 – 363Combined sources8
Beta strandi366 – 370Combined sources5
Turni376 – 378Combined sources3
Beta strandi380 – 387Combined sources8
Helixi389 – 392Combined sources4
Turni393 – 396Combined sources4
Helixi399 – 413Combined sources15
Helixi418 – 423Combined sources6
Beta strandi425 – 433Combined sources9
Turni437 – 439Combined sources3
Beta strandi440 – 444Combined sources5
Helixi450 – 459Combined sources10
Beta strandi463 – 467Combined sources5
Turni470 – 472Combined sources3
Beta strandi473 – 477Combined sources5
Helixi480 – 483Combined sources4
Helixi488 – 495Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4E0VX-ray3.10A/B1-497[»]
ProteinModelPortaliQ6TGQ9.
SMRiQ6TGQ9.
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.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.

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)DescriptionActionsGraphical viewLength
Non-terminal residuei4971

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY398691 mRNA. Translation: AAR31182.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY398691 mRNA. Translation: AAR31182.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4E0VX-ray3.10A/B1-497[»]
ProteinModelPortaliQ6TGQ9.
SMRiQ6TGQ9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005729.

Enzyme and pathway databases

BRENDAi1.4.3.2. 911.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 60 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

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.