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Protein

L-amino-acid oxidase

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

FAD1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei69FAD1 Publication1
Metal bindingi73Zinc1
Binding sitei88SubstrateBy similarity1
Binding sitei221SubstrateBy similarity1
Binding sitei259FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi277Zinc1
Binding sitei370SubstrateBy similarity1
Binding sitei455FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi41 – 42FAD1 Publication2
Nucleotide bindingi61 – 62FAD1 Publication2
Nucleotide bindingi85 – 88FAD1 Publication4
Nucleotide bindingi462 – 467FAD1 Publication6
Nucleotide bindingi462 – 463SubstrateBy similarity2
Nucleotide bindingi464 – 467FAD1 Publication4

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, 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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004125911 – 484L-amino-acid oxidaseAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi8 ↔ 1711 Publication
Glycosylationi170N-linked (GlcNAc...)1 Publication1
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

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Helixi14 – 23Combined sources10
Beta strandi33 – 37Combined sources5
Helixi41 – 52Combined sources12
Beta strandi56 – 60Combined sources5
Beta strandi62 – 67Combined sources6
Beta strandi72 – 75Combined sources4
Turni76 – 79Combined sources4
Beta strandi80 – 85Combined sources6
Helixi94 – 102Combined sources9
Beta strandi107 – 110Combined sources4
Beta strandi117 – 121Combined sources5
Beta strandi124 – 127Combined sources4
Helixi128 – 133Combined sources6
Helixi135 – 138Combined sources4
Helixi144 – 146Combined sources3
Helixi151 – 158Combined sources8
Helixi160 – 166Combined sources7
Helixi171 – 177Combined sources7
Helixi178 – 180Combined sources3
Helixi183 – 189Combined sources7
Helixi195 – 204Combined sources10
Helixi208 – 210Combined sources3
Helixi215 – 225Combined sources11
Beta strandi231 – 234Combined sources4
Helixi240 – 248Combined sources9
Helixi249 – 252Combined sources4
Beta strandi253 – 256Combined sources4
Beta strandi258 – 264Combined sources7
Beta strandi269 – 274Combined sources6
Beta strandi276 – 278Combined sources3
Beta strandi281 – 290Combined sources10
Helixi294 – 297Combined sources4
Beta strandi300 – 304Combined sources5
Helixi308 – 316Combined sources9
Beta strandi322 – 331Combined sources10
Helixi333 – 337Combined sources5
Beta strandi341 – 348Combined sources8
Beta strandi352 – 354Combined sources3
Beta strandi365 – 372Combined sources8
Helixi373 – 380Combined sources8
Helixi384 – 399Combined sources16
Helixi403 – 409Combined sources7
Beta strandi410 – 417Combined sources8
Helixi418 – 420Combined sources3
Turni422 – 424Combined sources3
Beta strandi425 – 429Combined sources5
Helixi435 – 444Combined sources10
Beta strandi450 – 452Combined sources3
Helixi455 – 457Combined sources3
Beta strandi458 – 462Combined sources5
Helixi464 – 481Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KVEX-ray2.57A/B/C/D1-484[»]
ProteinModelPortaliP0DI84.
SMRiP0DI84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0DI84.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.

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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KVEX-ray2.57A/B/C/D1-484[»]
ProteinModelPortaliP0DI84.
SMRiP0DI84.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0DI84.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 20 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

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.