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O93364

- OXLA_CROAD

UniProt

O93364 - OXLA_CROAD

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Protein
L-amino-acid oxidase
Gene
N/A
Organism
Crotalus adamanteus (Eastern diamondback rattlesnake)
Status
Reviewed - Annotation score: 4 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. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

FAD By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD By similarity
Binding sitei106 – 1061Substrate By similarity
Binding sitei239 – 2391Substrate By similarity
Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei390 – 3901Substrate By similarity
Binding sitei475 – 4751FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FAD By similarity
Nucleotide bindingi81 – 822FAD By similarity
Nucleotide bindingi103 – 1064FAD By similarity
Nucleotide bindingi482 – 4876FAD By similarity
Nucleotide bindingi482 – 4832Substrate By 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
Alternative name(s):
Apoxin I
Apoxin-1
OrganismiCrotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifieri8729 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 Publication
Add
BLAST
Chaini19 – 516498L-amino-acid oxidase
PRO_0000001706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 189 By similarity
Disulfide bondi349 ↔ 430 By similarity
Glycosylationi379 – 3791N-linked (GlcNAc...) Reviewed prediction

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

ProteinModelPortaliO93364.
SMRiO93364. Positions 21-503.

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.

O93364-1 [UniParc]FASTAAdd to Basket

« Hide

MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN    50
PKRVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA 100
NLGPMRLPTK HRIVREYIKK FDLKLNEFSQ ENENAWYFIK NIRKRVREVK 150
NNPGLLEYPV KPSEEGKSAA QLYVESLRKV VEELRSTNCK YILDKYDTYS 200
TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD 250
EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 300
SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT 350
KKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ 400
ALDFKDCADI VINDLSLIHE LPKEDIQTFC HPSMIQRWSL DKYAMGGITT 450
FTPYQFQHFS EALTAPFKRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR 500
ASENPSGIHL SNDNEF 516
Length:516
Mass (Da):58,662
Last modified:November 1, 1998 - v1
Checksum:iFDFAA77A49FDA05A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071564 mRNA. Translation: AAC32267.1.
PIRiJE0266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071564 mRNA. Translation: AAC32267.1 .
PIRi JE0266.

3D structure databases

ProteinModelPortali O93364.
SMRi O93364. 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. "Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein."
    Raibekas A.A., Massey V.
    Biochem. Biophys. Res. Commun. 248:476-478(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-44 AND 106-130.
    Tissue: Venom and Venom gland.
  2. "On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase."
    Massey V., Curti B.
    J. Biol. Chem. 242:1259-1264(1967) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_CROAD
AccessioniPrimary (citable) accession number: O93364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 78 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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