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Q6IWZ0

- OXLA_APLCA

UniProt

Q6IWZ0 - OXLA_APLCA

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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Aplysia californica (California sea hare)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.3 Publications

Cofactori

FAD1 Publication

Kineticsi

  1. KM=85.5 µM for L-Lys1 Publication
  2. KM=120.5 µM for L-Arg1 Publication

Vmax=4.5 µmol/sec/µg enzyme with L-Lys as substrate1 Publication

Vmax=5.5 µmol/sec/µg enzyme with L-Arg as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741FADBy similarity
Binding sitei94 – 941SubstrateBy similarity
Binding sitei406 – 4061SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 472FADBy similarity
Nucleotide bindingi66 – 672FADBy similarity
Nucleotide bindingi91 – 944FADBy similarity
Nucleotide bindingi513 – 5186FADBy similarity
Nucleotide bindingi513 – 5142SubstrateBy similarity

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB

GO - Biological processi

  1. defense response Source: UniProtKB
  2. defense response to bacterium Source: UniProtKB
  3. defense response to fungus Source: UniProtKB-KW
  4. killing of cells of other organism Source: UniProtKB-KW
  5. oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.2. 629.

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase1 Publication (EC:1.4.3.23 Publications)
Short name:
LAAO1 Publication
Short name:
LAOBy similarity
Alternative name(s):
Escapin1 Publication
OrganismiAplysia californica (California sea hare)
Taxonomic identifieri6500 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 535517L-amino-acid oxidase1 PublicationPRO_5000093471Add
BLAST

Post-translational modificationi

Not glycosylated.1 Publication

Expressioni

Tissue specificityi

Expressed exclusively in the ink gland. Within the ink gland, it is only detected in amber vesicles (at protein level).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ6IWZ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Sequence Analysis

Keywords - Domaini

Signal

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.

Q6IWZ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSAFLLLAC ALVISVHADG VCRNRRQCNK EVCGSSYDVA IVGAGPGGAN
60 70 80 90 100
SAYMLRESGL DIAVFEYSDR VGGRLFTYQL PNTPDVNLEI GGMRFIEGAM
110 120 130 140 150
HRLWKVISEL GLTPKVFKEG FGKEGRQRFY LRGQSLTKKQ VKSGDVPYDL
160 170 180 190 200
SPEEKANQGR LVEYYLEKLT GLQLNGGPLK REVALKLTVP DGRFLYDLTF
210 220 230 240 250
DEALDLVASP EGKEFARDTH VFTSEVTLDA SAISIFDDHL GEDYYGSEIY
260 270 280 290 300
TLEEGMSSVP QGLLQTFLDA AKSNEFFPNN HLKALRRRTN GQYVLYFEPT
310 320 330 340 350
TSKDGQTTIN YLEPLKVVCA QRVILAMPVY ALRQLDWSQL RNDRATQAYR
360 370 380 390 400
AVRPMPASKV FMTFDQPWWL QNERKSWVTK SDALFSQMYD WQKSEASGDY
410 420 430 440 450
ILIASYADGL KAQYLRELKN QGEDIPGSDP GYNQVTVPLK DAILEHLTEA
460 470 480 490 500
YGVERDSIPE PVTAASQFWT DYPFGCGWIT WRAGYHFDDV ISTMRRPSLK
510 520 530
DEVYVVGSDY SWGLISSWIE GALETSENVI NDYFL
Length:535
Mass (Da):60,300
Last modified:July 5, 2004 - v1
Checksum:i4F288F95F9B423FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY615888 mRNA. Translation: AAT12273.1.
RefSeqiNP_001191570.1. NM_001204641.2.
UniGeneiAcl.23634.

Genome annotation databases

GeneIDi100533346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY615888 mRNA. Translation: AAT12273.1 .
RefSeqi NP_001191570.1. NM_001204641.2.
UniGenei Acl.23634.

3D structure databases

ProteinModelPortali Q6IWZ0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100533346.

Enzyme and pathway databases

BRENDAi 1.4.3.2. 629.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: Ink1 Publication and Ink gland1 Publication.
  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: Ink1 Publication.
  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: Ink1 Publication.
  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.

Entry informationi

Entry nameiOXLA_APLCA
AccessioniPrimary (citable) accession number: Q6IWZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3