Reviewed, UniProtKB/Swiss-Prot Q6TGQ9 (OXLA_BOTJR)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2
Organism	Bothrops jararacussu (Jararacussu)
Taxonomic identifier	8726 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	497 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Inhibits platelet aggregation. Has an ability to induce apoptosis and hemorrhage. Has an antibacterial activity By similarity.
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated By similarity.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation
Cellular component	Secreted
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Oxidoreductase Toxin
PTM	Disulfide bond Glycoprotein
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 Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 13	13	By similarity
	Chain	14 – ›497	›484	L-amino-acid oxidase		PRO_0000273564
Regions
	Nucleotide binding	102 – 103	2	FAD By similarity
	Nucleotide binding	479 – 482	4	FAD By similarity
Sites
	Binding site	57	1	FAD By similarity
	Binding site	76	1	FAD By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	236	1	Substrate By similarity
	Binding site	274	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	385	1	Substrate By similarity
	Binding site	470	1	FAD By similarity
Amino acid modifications
	Glycosylation	185	1	N-linked (GlcNAc...) Potential
	Disulfide bond	23 ↔ 186		By similarity
	Disulfide bond	344 ↔ 425		By similarity
Experimental info
	Non-terminal residue	497	1

Sequences

	Sequence		Length	Mass (Da)
	Q6TGQ9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 51AFCB28038399A1	FASTA	497	56,289
	10 20 30 40 50 60 MNVFFMFSKP GKLADDRNPL EECFRETDYE EFLEIAKNGL STTSNPKRVV IVGAGMSGLS 70 80 90 100 110 120 AAYVLANAGH QVTVLEASER AGGQVKTYRN EKEGWYANLG PMRLPEKHRI VREYIRKFGL 130 140 150 160 170 180 QLNEFSQENE NAWYFIKNIR KRVGEVNKDP GVLDYPVKPS EVGKSAGQLY EESLQKAVEE 190 200 210 220 230 240 LRRTNCSYML NKYDTYSTKE YLLKEGNLSP GAVDMIGDLL NEDSGYYVSF IESLKHDDIF 250 260 270 280 290 300 AYEKRFDEIV GGMDKLPTSM YQAIQEKVHL NARVIKIQQD VKEVTVTYQT SEKETLSVTA 310 320 330 340 350 360 DYVIVCTTSR AARRIKFEPP LPPKKAHALR SVHYRSGTKI FLTCTKKFWE DDGIHGGKST 370 380 390 400 410 420 TDLPSRFIYY PNHNFPNGVG VIIAYGIGDD ANYFEALDFE DCGDIVINDL SLIHQLPKEE 430 440 450 460 470 480 IQAICRPSMI QRWSLDKYAM GGITTFTPYQ FQHFSEALTA PVDRIYFAGE YTAQAHGWIA 490 STIKSGPEGL DVNRASE

References

[1]

"Structural and functional characterization of L-amino acid oxidase from Bothrops jararacussu snake venom." Soares A.M., Kashima S., Roberto P.G., Astolfi-Filho S., Pereira J.O., Giglio J.R., Franca S.C. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY398691 mRNA. Translation: AAR31182.1.
3D structure databases
SMR	Q6TGQ9. Positions 17-497.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q6TGQ9.
Enzyme and pathway databases
BRENDA	1.4.3.2. 274601.
Family and domain databases
InterPro	IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00757. AMINEOXDASEF.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

OXLA_BOTJR

Accession

Primary (citable) accession number: Q6TGQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)