Reviewed, UniProtKB/Swiss-Prot O93364 (OXLA_CROAD)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2 Alternative name(s):     Apoxin-1     Apoxin I
Organism	Crotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifier	8729 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Has an antibacterial effect and an ability to induce apoptosis. The H2O2 produced by L-amino acid oxidation is involved apoptosis and hemorrhage caused by the venom By similarity.
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD.
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted.
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
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 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 – 18	18	Ref.1
	Chain	19 – 516	498	L-amino-acid oxidase		PRO_0000001706
Regions
	Nucleotide binding	105 – 106	2	FAD By similarity
	Nucleotide binding	484 – 487	4	FAD By similarity
Sites
	Binding site	81	1	FAD By similarity
	Binding site	89	1	FAD By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	239	1	Substrate By similarity
	Binding site	279	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	390	1	Substrate By similarity
	Binding site	475	1	FAD By similarity
Amino acid modifications
	Glycosylation	379	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 189		By similarity
	Disulfide bond	349 ↔ 430		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O93364-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: FDFAA77A49FDA05A	FASTA	516	58,662
	10 20 30 40 50 60 MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG 70 80 90 100 110 120 MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK 130 140 150 160 170 180 FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV 190 200 210 220 230 240 VEELRSTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD 250 260 270 280 290 300 DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 310 320 330 340 350 360 SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH 370 380 390 400 410 420 GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHE 430 440 450 460 470 480 LPKEDIQTFC HPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF 490 500 510 HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF

References

[1]

"Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein." Raibekas A.A., Massey V. Biochem. Biophys. Res. Commun. 248:476-478(1998) [PubMed: 9703950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-44 AND 106-130. Tissue: Venom and Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF071564 mRNA. Translation: AAC32267.1.
PIR	JE0266.
3D structure databases
HSSP	HSSP built from PDB template 1F8R based on UniProtKB P81382.
SMR	O93364. Positions 22-504.
ModBase	Search...
Phylogenomic databases
HOVERGEN	O93364.
Enzyme and pathway databases
BRENDA	1.4.3.2. 18620.
Family and domain databases
InterPro	IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

OXLA_CROAD

Accession

Primary (citable) accession number: O93364

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)