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A8QL52

- OXLA_BUNFA

UniProt

A8QL52 - OXLA_BUNFA

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Protein
L-amino-acid oxidase
Gene
N/A
Organism
Bungarus fasciatus (Banded krait)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active against L-Lys, L-Arg, L-Ala and L-Asn), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as edema, inflammatory cell infiltration, cytotoxicity and apoptosis, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, and have antibacterial and antiparasitic activities.1 Publication

Catalytic activityi

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

Cofactori

FAD By similarity.

Kineticsi

  1. KM=28.28 mM for L-Ala1 Publication
  2. KM=18.75 mM for L-Arg
  3. KM=0.04 mM for L-Asp
  4. KM=19.07 mM for L-Asn
  5. KM=5.88 mM for L-Gln
  6. KM=1.44 mM for L-Glu
  7. KM=4.84 mM for L-His
  8. KM=1.64 mM for L-Ile
  9. KM=60.69 mM for L-Leu
  10. KM=21.49 mM for L-Lys
  11. KM=15.03 mM for L-Met
  12. KM=0.13 mM for L-Phe
  13. KM=0.27 mM for L-Trp
  14. KM=0.05 mM for L-Tyr

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901FAD By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei280 – 2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei391 – 3911Substrate By similarity
Binding sitei476 – 4761FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 632FAD By similarity
Nucleotide bindingi82 – 832FAD By similarity
Nucleotide bindingi106 – 1094FAD By similarity
Nucleotide bindingi483 – 4886FAD By similarity
Nucleotide bindingi483 – 4842Substrate 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, Platelet aggregation activating toxin, 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:
Bf-LAAO
Short name:
LAAO
Short name:
LAO
OrganismiBungarus fasciatus (Banded krait)
Taxonomic identifieri8613 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

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 – 19191 Publication
Add
BLAST
Chaini20 – 517498L-amino-acid oxidase
PRO_0000412599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 192 By similarity
Glycosylationi191 – 1911N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi350 ↔ 431 By similarity
Glycosylationi380 – 3801N-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

Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA8QL52.
SMRiA8QL52. Positions 23-505.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A8QL52-1 [UniParc]FASTAAdd to Basket

« Hide

MNVFSIFSLV FLAAFGSCAD DRRSALEECF READYEEFLE IARNGLKKTS    50
NPKHVVVVGA GMAGLSAAYV LAGAGHRVTL LEASDRVGGR VNTYRDEKEG 100
WYVNMGPMRL PERHRIVRTY IAKFGLKLNE FFQENENAWY FIRNIRKRVW 150
EVKKDPGVFK YPVKPSEEGK SASQLYRESL KKVIEELKRT NCSYILDKYD 200
TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL KNDDLFSYEK 250
RFDEISDGFD QLPKSMHQAI AEMVHLNAQV IKIQRDAEKV RVAYQTPAKT 300
LSYVTADYVI VCATSRAVRR ISFEPPLPPK KAHALRSIHY KSATKIFLTC 350
TRKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YVLADDSDFF 400
QALDIKTSAD IVINDLSLIH QLPKNEIQAL CYPSLIKKWS LDKYTMGALT 450
SFTPYQFQDY IETVAAPVGR IYFAGEYTAT VHGWLDSTIK SGLTAARNVN 500
RASQKPSRIH LINDNQL 517
Length:517
Mass (Da):58,764
Last modified:January 15, 2008 - v1
Checksum:iE869950FB941B11D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF080833 mRNA. Translation: ABN72540.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF080833 mRNA. Translation: ABN72540.1 .

3D structure databases

ProteinModelPortali A8QL52.
SMRi A8QL52. Positions 23-505.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005729.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00757. AMINEOXDASEF.
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of L-amino acid oxidase from king cobra venom."
    Jin Y., Lee W.-H., Zeng L., Zhang Y.
    Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom."
    Wei J.-F., Yang H.-W., Wei X.-L., Qiao L.-Y., Wang W.-Y., He S.-H.
    Toxicon 54:262-271(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-36, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_BUNFA
AccessioniPrimary (citable) accession number: A8QL52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein 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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