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Q6IWZ0 (OXLA_APLCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
EC=1.4.3.2
Alternative name(s):
Escapin
OrganismAplysia californica (California sea hare)
Taxonomic identifier6500 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidative deamination of positively charged L-amino acids L-Lys and L-Arg and, much less efficiently, of amino acids L-His and L-Tyr. Has antimicrobial activity. Inhibits growth of Gram-negative bacteria E.coli strain MC4100 (MIC=0.62 µg/ml), E.coli strain C921-b2, S.typhimurium strain AA 140 (MIC=0.62 µg/ml), P.aeruginosa strain PAO1 (MIC=0.31 µg/ml) and V.harveyi strain BB170 (MIC=0.25 µg/ml). Inhibits growth of Gram-positive bacteria S.aureus stain 6835 (MIC=0.31 µg/ml), S.pyogenes strain NZ131 (MIC=0.62 µg/ml), B.subtilis strain 168 (MIC=2.50 µg/ml) and B.subtilis strain WB600 (MIC=2.50 µg/ml). The antibacterial effect can be bacteriostatic, mediated mostly by H2O2, as well as bactericidal. The latter appears to be due to unstable intermediates generated from alpha-keto-epsilon-aminocaproic acid, an intermediate of escapin-deaminated L-Lys, and H2O2. The bactericidal effect is stronger at lower pH levels. Intermediates generated from L-Arg have no bactericidal effect. Inhibits growth of yeast species S.cerevisiae strain BY4761 (MIC=5.0 µg/ml) and C.krusei (MIC=5.0 µg/ml). Inhibits growth of C.sphaerospermum in a lysine-dependent manner. As components of ink, products from escapin's enzymatic activity may play a role in deterring eukaryotic predators. Ref.1 Ref.2 Ref.3 Ref.5

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5

Cofactor

FAD. Ref.1 Ref.5

Subcellular location

Secreted Ref.2.

Tissue specificity

Expressed exclusively in the ink gland. Within the ink gland, it is only detected in amber vesicles (at protein level). Ref.2

Post-translational modification

Not glycosylated. Ref.1 Ref.5

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=85.5 µM for L-Lys Ref.1 Ref.5

KM=120.5 µM for L-Arg Ref.5

Vmax=4.5 µmol/sec/µg enzyme with L-Lys as substrate Ref.5

Vmax=5.5 µmol/sec/µg enzyme with L-Arg as substrate Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.5
Chain19 – 535517L-amino-acid oxidase Ref.5
PRO_5000093471

Regions

Nucleotide binding46 – 472FAD By similarity UniProtKB P81382
Nucleotide binding66 – 672FAD By similarity UniProtKB P81382
Nucleotide binding91 – 944FAD By similarity UniProtKB P81382
Nucleotide binding513 – 5186FAD By similarity UniProtKB P81382
Nucleotide binding513 – 5142Substrate By similarity UniProtKB P81382

Sites

Binding site741FAD By similarity UniProtKB P81382
Binding site941Substrate By similarity UniProtKB P81382
Binding site4061Substrate By similarity UniProtKB P81382

Sequences

Sequence LengthMass (Da)Tools
Q6IWZ0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4F288F95F9B423FC

FASTA53560,300
        10         20         30         40         50         60 
MSSAFLLLAC ALVISVHADG VCRNRRQCNK EVCGSSYDVA IVGAGPGGAN SAYMLRESGL 

        70         80         90        100        110        120 
DIAVFEYSDR VGGRLFTYQL PNTPDVNLEI GGMRFIEGAM HRLWKVISEL GLTPKVFKEG 

       130        140        150        160        170        180 
FGKEGRQRFY LRGQSLTKKQ VKSGDVPYDL SPEEKANQGR LVEYYLEKLT GLQLNGGPLK 

       190        200        210        220        230        240 
REVALKLTVP DGRFLYDLTF DEALDLVASP EGKEFARDTH VFTSEVTLDA SAISIFDDHL 

       250        260        270        280        290        300 
GEDYYGSEIY TLEEGMSSVP QGLLQTFLDA AKSNEFFPNN HLKALRRRTN GQYVLYFEPT 

       310        320        330        340        350        360 
TSKDGQTTIN YLEPLKVVCA QRVILAMPVY ALRQLDWSQL RNDRATQAYR AVRPMPASKV 

       370        380        390        400        410        420 
FMTFDQPWWL QNERKSWVTK SDALFSQMYD WQKSEASGDY ILIASYADGL KAQYLRELKN 

       430        440        450        460        470        480 
QGEDIPGSDP GYNQVTVPLK DAILEHLTEA YGVERDSIPE PVTAASQFWT DYPFGCGWIT 

       490        500        510        520        530 
WRAGYHFDDV ISTMRRPSLK DEVYVVGSDY SWGLISSWIE GALETSENVI NDYFL 

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ABSENCE OF GLYCOSYLATION.
Tissue: Ink and Ink gland.
[2]"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.
[3]"Identification of potent bactericidal compounds produced by escapin, an L-amino acid oxidase in the ink of the sea hare Aplysia californica."
Ko K.C., Wang B., Tai P.C., Derby C.D.
Antimicrob. Agents Chemother. 52:4455-4462(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
Tissue: Ink.
[4]"The chemistry of escapin: identification and quantification of the components in the complex mixture generated by an L-amino acid oxidase in the defensive secretion of the sea snail Aplysia californica."
Kamio M., Ko K.C., Zheng S., Wang B., Collins S.L., Gadda G., Tai P.C., Derby C.D.
Chemistry 15:1597-1603(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
Tissue: Ink.
[5]"Effects of sea hare ink secretion and its escapin-generated components on a variety of predatory fishes."
Nusnbaum M., Derby C.D.
Biol. Bull. 218:282-292(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY615888 mRNA. Translation: AAT12273.1.
RefSeqNP_001191570.1. NM_001204641.1.
UniGeneAcl.23634.

3D structure databases

ProteinModelPortalQ6IWZ0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100533346.

Enzyme and pathway databases

BRENDA1.4.3.2. 629.

Family and domain databases

InterProIPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOXLA_APLCA
AccessionPrimary (citable) accession number: Q6IWZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families