Reviewed, UniProtKB/Swiss-Prot Q4F867 (OXLA_DABRU)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=DRS-LAAO       Short name=LAAO       Short name=LAO     EC=1.4.3.2
Organism	Daboia russelli siamensis (Eastern Russell's viper) (Daboia russelli formensis)
Taxonomic identifier	343250 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Daboia

Protein attributes

Sequence length	407 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Displays high specificity towards L-Leu followed by L-Phe and L-Ile, while five substrates L-Pro, L-Asn, L-Gly, L-Ser and L-Cys are not oxidized. Does not show hemorrhagic activity. Dose-dependently inhibits platelet aggregation induced by ADP and TMVA. Has antibacterial activity against S.aureus (ATCC 25923) (MIC=9.0 µg/ml), P.aeruginosa (ATCC 27853) (MIC=144.0 µg/ml) and E.coli (ATCC 25922) (MIC=288.0 µg/ml). The hydrogen peroxide produced by L-amino acid oxidation may be partly involved in platelet aggregation inhibition and antimicrobial activities.
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer; not disulfid-linked.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 8.8.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Oxidoreductase Toxin
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Ref.1 Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Ref.1 Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Ref.1 Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-amino-acid oxidase activity Ref.1 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 407	407	L-amino-acid oxidase		PRO_0000315372
Regions
	Nucleotide binding	378 – 390	13	FAD By similarity
Sites
	Binding site	144	1	Substrate By similarity
	Binding site	182	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	293	1	Substrate By similarity
Amino acid modifications
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	282	1	N-linked (GlcNAc...) Potential
	Disulfide bond	10 ↔ 94		By similarity
	Disulfide bond	252 ↔ 333		By similarity
Experimental info
	Non-adjacent residues	15 – 16	2
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q4F867-1 [UniParc]. Last modified January 19, 2010. Version 2. Checksum: 8B7B22226EF561B9	FASTA	407	46,372
	10 20 30 40 50 60 ADDKNPLEEC FREDDHRIVR EYIRKFGLKL NEFVQETENG WYFIKNIRKR VGEVKKDPGL 70 80 90 100 110 120 LKYPVKPSEA GKSAGQLYQE SLGKAVEELK RTNCSYILNK YDTYSTKEYL IKEGNLSPGA 130 140 150 160 170 180 VDMIGDLLNE DSGYYVSFIE SLKHDDIFAY EKRFDEIVGG MDQLPTSMYR AIEESVRFKA 190 200 210 220 230 240 RVIKIQQNAE KVTVTYQTTQ KNLLLETVDY VIVCTTSRAA RRITFKPPLP PKKAHALRSV 250 260 270 280 290 300 HYRSGTKIFL TCTKKFWEDD GIQGGKSTTD LPSRFIYYPN HNFTTGVGVI IAYGIGDDAN 310 320 330 340 350 360 FFQALNLNEC ADIVFNDLSS IHQLPKKDLQ TFCYPSIIQK WSLDKYAMGA ITTFTPYQFQ 370 380 390 400 HFSEALTAPV GRIFFAGEYT ANAHGWIDST IKSGLTAARD VNRASEL

References

[1]

"Purification and characterization of a new L-amino acid oxidase from Daboia russellii siamensis venom." Zhong S.-R., Jin Y., Wu J.-B., Jia Y.-H., Xu G.-L., Wang G.-C., Xiong Y.-L., Lu Q.-M. Toxicon 54:763-771(2009) [PubMed: 19523971] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, NUCLEOTIDE SEQUENCE [MRNA] OF 16-407, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Venom and Venom gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ104365 mRNA. Translation: AAZ08620.1.
3D structure databases
SMR	Q4F867. Positions 1-391.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q4F867.
Family and domain databases
InterPro	IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OXLA_DABRU

Accession

Primary (citable) accession number: Q4F867

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 19, 2010
Last modified:	January 19, 2010
This is version 17 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)