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Q6IWZ0

- OXLA_APLCA

UniProt

Q6IWZ0 - OXLA_APLCA

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
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    FAD.1 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

    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

    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

    MSSAFLLLAC ALVISVHADG VCRNRRQCNK EVCGSSYDVA IVGAGPGGAN    50
    SAYMLRESGL DIAVFEYSDR VGGRLFTYQL PNTPDVNLEI GGMRFIEGAM 100
    HRLWKVISEL GLTPKVFKEG FGKEGRQRFY LRGQSLTKKQ VKSGDVPYDL 150
    SPEEKANQGR LVEYYLEKLT GLQLNGGPLK REVALKLTVP DGRFLYDLTF 200
    DEALDLVASP EGKEFARDTH VFTSEVTLDA SAISIFDDHL GEDYYGSEIY 250
    TLEEGMSSVP QGLLQTFLDA AKSNEFFPNN HLKALRRRTN GQYVLYFEPT 300
    TSKDGQTTIN YLEPLKVVCA QRVILAMPVY ALRQLDWSQL RNDRATQAYR 350
    AVRPMPASKV FMTFDQPWWL QNERKSWVTK SDALFSQMYD WQKSEASGDY 400
    ILIASYADGL KAQYLRELKN QGEDIPGSDP GYNQVTVPLK DAILEHLTEA 450
    YGVERDSIPE PVTAASQFWT DYPFGCGWIT WRAGYHFDDV ISTMRRPSLK 500
    DEVYVVGSDY SWGLISSWIE GALETSENVI NDYFL 535
    Length:535
    Mass (Da):60,300
    Last modified:July 5, 2004 - v1
    Checksum:i4F288F95F9B423FC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY615888 mRNA. Translation: AAT12273.1.
    RefSeqiNP_001191570.1. NM_001204641.1.
    UniGeneiAcl.23634.

    Genome annotation databases

    GeneIDi100533346.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY615888 mRNA. Translation: AAT12273.1 .
    RefSeqi NP_001191570.1. NM_001204641.1.
    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: October 1, 2014
    This is version 32 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