NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, AND MASS SPECTROMETRY.
TISSUE=Venom, and Venom gland;
DOI=10.1016/j.bbrc.2003.08.044; PubMed=12963032 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y.;
"Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity.";
Biochem. Biophys. Res. Commun. 309:598-604(2003).

[2]

NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Wang J., Huang Q., Teng M., Niu L.;
"Purification, cloning and characterization of the L-amino acid oxidase in snake Trimeresurus stejnegeri.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.

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). Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication.
CATALYTIC ACTIVITY: An L-amino acid + H₂O + O₂ = a 2-oxo acid + NH₃ + H₂O₂.
COFACTOR: FAD (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted (By similarity).
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Glycosylated.
SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY277739; AAQ56232.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY338966; AAQ16182.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P81382; 1F8R. [HSSP ENTRY / PDB]

SMR

Q6WP39; 22-504.

ModBase

Q6WP39.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR001613; Amineoxid_fl.
IPR002937; Amino_oxidase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
Graphical view of domain structure.

Pfam

PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.
PR00757; AMINEOXDASEF.
PR00368; FADPNR.

BLOCKS

Q6WP39.

Phylogenomic databases

HOVERGEN

Q6WP39; -.

Other

ProtoNet

Q6WP39.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic; Antimicrobial; Antiviral protein; Apoptosis; Blood coagulation; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`By similarity.`
`CHAIN`	`19 516`	`498`	`L-amino-acid oxidase.`	`PRO_0000273572`
`NP_BIND`	`107 108`	`2`	`FAD (By similarity).`
`NP_BIND`	`484 487`	`4`	`FAD (By similarity).`
`BINDING`	`62 62`		`FAD (By similarity).`
`BINDING`	`81 81`		`FAD (By similarity).`
`BINDING`	`89 89`		`FAD (By similarity).`
`BINDING`	`108 108`		`Substrate (By similarity).`
`BINDING`	`241 241`		`Substrate (By similarity).`
`BINDING`	`279 279`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`390 390`		`Substrate (By similarity).`
`BINDING`	`475 475`		`FAD (By similarity).`
`CARBOHYD`	`190 190`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`379 379`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`28 191`		`By similarity.`
`DISULFID`	`349 430`		`By similarity.`
`CONFLICT`	`16 16`		`G -> E (in Ref. 2; AAQ16182).`
`CONFLICT`	`53 53`		`H -> R (in Ref. 2; AAQ16182).`
`CONFLICT`	`73 73`		`A -> T (in Ref. 2; AAQ16182).`
`CONFLICT`	`181 181`		`K -> E (in Ref. 2; AAQ16182).`
`CONFLICT`	`294 294`		`H -> Q (in Ref. 2; AAQ16182).`
`CONFLICT`	`315 315`		`R -> G (in Ref. 2; AAQ16182).`
`CONFLICT`	`354 354`		`R -> W (in Ref. 2; AAQ16182).`
`CONFLICT`	`514 514`		`D -> N (in Ref. 2; AAQ16182).`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 58601 Da [This is the MW of the unprocessed precursor]

CRC64: FB5AC0BC171B9288 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFNLQLNEF SQENDNAWHF VKNIRKTVGE VKKDPGVLKY PVKPSEEGKS AEQLYEESLR 

       190        200        210        220        230        240 
KVEKELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT 

       310        320        330        340        350        360 
SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT KKFREDEGIH 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDLKDCGDI VINDLSLIHQ 

       430        440        450        460        470        480 
LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EALTSHVDRI YFAGEYTAHA 

       490        500        510 
HGWIDSSIKS GLTAARDVNR ASENPSGIHL SNDDEL

Q6WP39 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools