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P0DI84

- OXLA_VIPAA

UniProt

P0DI84 - OXLA_VIPAA

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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Vipera ammodytes ammodytes (Western sand viper)
Status
Reviewed - Annotation score: 5 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691FAD1 Publication
Metal bindingi73 – 731Zinc
Binding sitei88 – 881SubstrateBy similarity
Binding sitei221 – 2211SubstrateBy similarity
Binding sitei259 – 2591FAD; via amide nitrogen and carbonyl oxygen1 Publication
Metal bindingi277 – 2771Zinc
Binding sitei370 – 3701SubstrateBy similarity
Binding sitei455 – 4551FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 422FAD1 Publication
Nucleotide bindingi61 – 622FAD1 Publication
Nucleotide bindingi85 – 884FAD1 Publication
Nucleotide bindingi462 – 4676FAD1 Publication
Nucleotide bindingi462 – 4632SubstrateBy similarity
Nucleotide bindingi464 – 4674FAD1 Publication

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

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, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
Short name:
VAA-LAAO I
OrganismiVipera ammodytes ammodytes (Western sand viper)
Taxonomic identifieri8705 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

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
Chaini1 – 484484L-amino-acid oxidasePRO_0000412591Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi8 ↔ 1711 Publication
Glycosylationi170 – 1701N-linked (GlcNAc...)1 Publication
Disulfide bondi329 ↔ 4101 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.1 Publication

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94
Helixi14 – 2310
Beta strandi33 – 375
Helixi41 – 5212
Beta strandi56 – 605
Beta strandi62 – 676
Beta strandi72 – 754
Turni76 – 794
Beta strandi80 – 856
Helixi94 – 1029
Beta strandi107 – 1104
Beta strandi117 – 1215
Beta strandi124 – 1274
Helixi128 – 1336
Helixi135 – 1384
Helixi144 – 1463
Helixi151 – 1588
Helixi160 – 1667
Helixi171 – 1777
Helixi178 – 1803
Helixi183 – 1897
Helixi195 – 20410
Helixi208 – 2103
Helixi215 – 22511
Beta strandi231 – 2344
Helixi240 – 2489
Helixi249 – 2524
Beta strandi253 – 2564
Beta strandi258 – 2647
Beta strandi269 – 2746
Beta strandi276 – 2783
Beta strandi281 – 29010
Helixi294 – 2974
Beta strandi300 – 3045
Helixi308 – 3169
Beta strandi322 – 33110
Helixi333 – 3375
Beta strandi341 – 3488
Beta strandi352 – 3543
Beta strandi365 – 3728
Helixi373 – 3808
Helixi384 – 39916
Helixi403 – 4097
Beta strandi410 – 4178
Helixi418 – 4203
Turni422 – 4243
Beta strandi425 – 4295
Helixi435 – 44410
Beta strandi450 – 4523
Helixi455 – 4573
Beta strandi458 – 4625
Helixi464 – 48118

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KVEX-ray2.57A/B/C/D1-484[»]
ProteinModelPortaliP0DI84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0DI84.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

P0DI84-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
DRNPLEECFR ETDYEEFLEI ARNGLKKTSN PKHVVVVGAG MSGLSAAYVL
60 70 80 90 100
AGAGHKVTVL EASERAGGRV RTHRNSKEGW YANLGPMRIP EKHRIVREYI
110 120 130 140 150
RKFGLNLNEF SQENDNAWYF IKNIRKRVGE VNKDPGLLKY PVKPSEEGKS
160 170 180 190 200
AGQLYEESLG SAVKDLKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM
210 220 230 240 250
IGDLLNEDSG YYVSFIESLK HDDIFAYEKR FDEIVGGMDQ LPTSMYRAIE
260 270 280 290 300
EKVKFNARVI KIQQNANQVT VTYQTPEKDT SSNTADYVIV CTTSRAARRI
310 320 330 340 350
QFEPPLPPKK QHALRSVHYR SGTKIFLTCS SKFWEDDGIH GGKSTTDLPS
360 370 380 390 400
RFIYYPNHNF STGVGVIIAY GIGDDANFFQ ALKFKDCADI VFNDLSLIHQ
410 420 430 440 450
LPKEEIQSFC YPSMIQKWSL DKYAMGAITT FTPYQFQRFS EALTAPQGRI
460 470 480
FFAGEYTAEA HGWIDSTIKS GLTAARDVNR ASEQ
Length:484
Mass (Da):54,748
Last modified:September 21, 2011 - v1
Checksum:iFF2BBFB0EB5D1C47
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3KVE X-ray 2.57 A/B/C/D 1-484 [» ]
ProteinModelPortali P0DI84.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0DI84.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00757. AMINEOXDASEF.
ProtoNeti Search...

Publicationsi

  1. "Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom."
    Georgieva D., Kardas A., Buck F., Perbandt M., Betzel C.
    Acta Crystallogr. F 64:918-921(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION.
    Tissue: Venom.
  2. "Comparative analysis of the venom proteomes of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis."
    Georgieva D., Risch M., Kardas A., Buck F., von Bergen M., Betzel C.
    J. Proteome Res. 7:866-886(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom.
  3. "The structure of a native L-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions."
    Georgieva D., Murakami M., Perband M., Arni R., Betzel C.
    Mol. Biosyst. 7:379-384(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH FAD AND ZINC IONS, COFACTOR, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-170.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_VIPAA
AccessioniPrimary (citable) accession number: P0DI84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: October 29, 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

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