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P86163 (OXLA_APLDA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 4. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
EC=1.4.3.2
Alternative name(s):
Dactylomelin-P
OrganismAplysia dactylomela (Spotted sea hare)
Taxonomic identifier144766 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

Protein attributes

Sequence length26 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidative deamination of positively charged L-amino acids L-Lys and L-Arg but not of amino acids L-His, L-Asp or L-Glu. Has antibacterial activity against the Gram-positive bacterium S.aureus (MIC=15 µg/ml). This antibacterial activity is bacteriostatic in the absence of amino acids L-Lys or L-Arg but bactericidal in their presence. The antibacterial effect is largely dependent on H2O2 produced in the oxidative deamination of substrates. Has hemagglutinating activity towards rabbit erythrocytes. Hemagglutinating activity is inhibited by the glycoprotein fetuin, but not by glucose, mannose, galactose, N-acetylglucosamine, N-acetylgalactosamine or sialic acid. Ref.1 Ref.2

Catalytic activity

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

Cofactor

FAD. Ref.1

Subunit structure

Monomer. Ref.2

Subcellular location

Secreted Ref.1 Ref.2 Ref.4.

Tissue specificity

Expressed by the ink gland. Ref.4

Post-translational modification

Not glycosylated. Ref.2 Ref.3

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.22 mM for L-Lys Ref.1

KM=0.015 mM for L-Arg Ref.1

pH dependence:

Optimum pH is 8. More than 50% activity is retained between pH 3 and 12. Inactive at pH 2. Ref.1

Temperature dependence:

Activity remains stable after 30 min at 55 degrees Celsius. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›26›26L-amino-acid oxidase
PRO_0000413471

Experimental info

Non-terminal residue261

Sequences

Sequence LengthMass (Da)Tools
P86163 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 9B38D1C8D14C510E

FASTA262,731
        10         20 
DGVCSNRRQC NKEVCGSSYD VAIVGA 

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References

[1]"Further characterization and mode of action of dactylomelin-P, an antibacterial protein isolated from the ink of the sea hare Aplysia dactylomela (Rang, 1828)."
Tavares T.C.L., Nogueira V.L.R., Vasconcelos I.M., Gomes V.M., da Cunha M., Carvalho A.F.U., Melo V.M.M.
J. Exp. Mar. Biol. Ecol. 0:0-0(2011)
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Tissue: Ink.
[2]"Purification of a novel antibacterial and haemagglutinating protein from the purple gland of the sea hare, Aplysia dactylomela rang, 1828."
Melo V.M.M., Duarte A.B.G., Carvalho A.F.F.U., Siebra E.A., Vasconcelos I.M.
Toxicon 38:1415-1427(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ABSENCE OF GLYCOSYLATION.
Tissue: Ink.
[3]"Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica."
Yang H., Johnson P.M., Ko K.C., Kamio M., Germann M.W., Derby C.D., Tai P.C.
J. Exp. Biol. 208:3609-3622(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSENCE OF GLYCOSYLATION.
[4]"Packaging of chemicals in the defensive secretory glands of the sea hare Aplysia californica."
Johnson P.M., Kicklighter C.E., Schmidt M., Kamio M., Yang H., Elkin D., Michel W.C., Tai P.C., Derby C.D.
J. Exp. Biol. 209:78-88(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Ink.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_APLDA
AccessionPrimary (citable) accession number: P86163
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: April 16, 2014
This is version 4 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families