Reviewed, UniProtKB/Swiss-Prot Q4JHE1 (OXLA_PSEAU)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2
Organism	Pseudechis australis (Mulga snake) (King brown snake)
Taxonomic identifier	8670 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Pseudechis

Protein attributes

Sequence length	517 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. Inhibits platelet aggregation. Has an ability to induce apoptosis and hemorrhage By similarity. Has an antibacterial activity.
Catalytic activity	An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
Cofactor	FAD By similarity.
Subunit structure	Homodimer. Ref.2
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	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-KW
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	By similarity
	Chain	19 – 517	499	L-amino-acid oxidase		PRO_5000140380
Regions
	Nucleotide binding	108 – 109	2	FAD By similarity
	Nucleotide binding	485 – 488	4	FAD By similarity
Sites
	Binding site	82	1	FAD By similarity
	Binding site	90	1	FAD By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	280	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	391	1	Substrate By similarity
	Binding site	476	1	FAD By similarity
Amino acid modifications
	Glycosylation	191	1	N-linked (GlcNAc...) Potential
	Disulfide bond	29 ↔ 192		By similarity
	Disulfide bond	350 ↔ 431		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4JHE1-1 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: 9E0ACCD728782BE5	FASTA	517	58,744
	10 20 30 40 50 60 MNVFFMFSLL FLAALGSCAD DRRRPLEECF READYEEFLE IAKNGLQRTS NPKRVVVVGA 70 80 90 100 110 120 GMAGLSAAYV LAGAGHQVTL LEASERVGGR VNTYRNEKDG WYVNLGPMRL PERHRIIREY 130 140 150 160 170 180 IRKFGLELNE FIQENDNAWY FIKNIRKRVS EVKKDPGVFK YPVKPSEEGK SASQLYRESL 190 200 210 220 230 240 QKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSPGAVD MIGDLLNEDS SYYLSFIESL 250 260 270 280 290 300 KSDDIFSYEK RFDEIVGGFD QLPRSMYQAI AEKVHLNAQV IKIQQNAEDV RVTYQTPAKT 310 320 330 340 350 360 LSYVIADYVI VCSTSRAARR IHFEPPLPPK KAHALRSIHY RSSTKIFLTC SQKFWEADGI 370 380 390 400 410 420 HGGKSTTDLP SRFIYYPNHS FTSGIGVIVA YTLADDTDFF QALDIETSAD IVINDLSLIH 430 440 450 460 470 480 QLPKEQIQAL CYPSKIQKWS LDEYAMGAIT SFTPYQFQDF FEIVAAPVGR IYFAGEYTAS 490 500 510 VHGWLDSTIK SGLTAARDVN LASQKPSRIQ LSNDNEL

References

[1]	"Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species." St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F. Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed: 16261251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom." Stiles B.G., Sexton F.W., Weinstein S.A. Toxicon 29:1129-1141(1991) [PubMed: 1796476] [Abstract] Cited for: FUNCTION, SUBUNIT. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ088992 mRNA. Translation: AAY89682.1.
3D structure databases
SMR	Q4JHE1. Positions 23-504.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q4JHE1.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00419. ADXRDTASE. PR00757. AMINEOXDASEF.
ProtoNet	Search...

Entry information

Entry name

OXLA_PSEAU

Accession

Primary (citable) accession number: Q4JHE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	August 2, 2005
Last modified:	November 25, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)