A6MFL0 (OXLA_DEMVE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=LAAO Short name=LAO EC=1.4.3.2
Organism	Demansia vestigiata (Lesser black whip snake) (Demansia atra)
Taxonomic identifier	412038 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Notechinae › Demansia

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 transcript level

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer; non-covalently linked By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	N-glycosylated By similarity.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation Cytolysis Hemolysis
Cellular component	Secreted
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Oxidoreductase Toxin
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 517	499	L-amino-acid oxidase		PRO_5000254114
Regions
	Nucleotide binding	62 – 63	2	FAD By similarity
	Nucleotide binding	82 – 83	2	FAD By similarity
	Nucleotide binding	106 – 109	4	FAD By similarity
	Nucleotide binding	483 – 488	6	FAD By similarity
	Nucleotide binding	483 – 484	2	Substrate By similarity
Sites
	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)
	A6MFL0 [UniParc]. Last modified July 24, 2007. Version 1. Checksum: 474BB53222E72C22	FASTA	517	58,920
	10 20 30 40 50 60 MNVFFMFSLL FLAALESCAD DRRNPLGECF READYEEFVD IATNGLKQTS NPKRVVVVGA 70 80 90 100 110 120 GMAGLSAAYV LAGAGHNVML LEASERVGGR VNTYRNEQEG WYVNLGPMRL PERHRIVREY 130 140 150 160 170 180 IKKFGLQLNQ FFQEDEDAWY FIKNIRKKVR EVKENPSIFP YPVKPSEKGK SAPQLYRDSL 190 200 210 220 230 240 QKIIEEYGRS NCSYILNKYD TYSTKDYLIK EGNLSPGAVD MIGDLLNEGS SYYLSFIESL 250 260 270 280 290 300 KSDDIFSYEN RFDEIVGGFD LLPKAMYKAI EEKVHLNARV IQIQQNAEGV RVTYQTPAKN 310 320 330 340 350 360 LSYVTADYVI VCSTSRAARR IYFEPPLPPE KAHALQSIHY RSATKIFLTC TKKFWEDDGI 370 380 390 400 410 420 HGGKSITDRP SRLIHYPNHN FPNGIGVLVI YTIADDADFF LALDNKTIAD IVIHDLSLIH 430 440 450 460 470 480 QLPKEKIRDL CYVSMIKKWS LDKYSMGSIT TFAPYQFQEY FETVAAPVGR IYFAGEYTAR 490 500 510 AHGWIDSTIK SGLKAARDVN RASQKPSRIQ LSNDNEL

References

[1]

"Diversity of toxic components from the venom of the evolutionarily distinct black whip snake, Demansia vestigiata." St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J., de Jersey J., Masci P.P., Lavin M.F. J. Proteome Res. 6:3093-3107(2007) [PubMed: 17608513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ917521 mRNA. Translation: ABK63550.1.
3D structure databases
ProteinModelPortal	A6MFL0.
SMR	A6MFL0. Positions 23-505.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG005729.
Family and domain databases
InterPro	IPR002937. Amino_oxidase. IPR001613. Flavin_amine_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00757. AMINEOXDASEF.
ProtoNet	Search...

Entry information

Entry name

OXLA_DEMVE

Accession

Primary (citable) accession number: A6MFL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 24, 2007
Last modified:	October 19, 2011
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program