[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-33. TISSUE=Venom, and Venom gland; PubMed=11248687 [NCBI, ExPASy, EBI, Israel, Japan] Macheroux P., Seth O., Bollschweiler C., Schwarz M., Kurfuerst M., Au L.-C., Ghisla S.; "L-amino-acid oxidase from Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzyme."; Eur. J. Biochem. 268:1679-1686(2001).
[2]	PROTEIN SEQUENCE OF 19-38, AND SUBUNIT. TISSUE=Venom; DOI=10.1006/abbi.1994.1401; PubMed=8080286 [NCBI, ExPASy, EBI, Israel, Japan] Ponnudurai G., Chung M.C.M., Tan N.-H.; "Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."; Arch. Biochem. Biophys. 313:373-378(1994).
[3]	EXPRESSION OF ACTIVE RECOMBINANT LAAO. DOI=10.1016/j.pep.2006.09.016; PubMed=17127077 [NCBI, ExPASy, EBI, Israel, Japan] Kommoju P.R., Macheroux P., Ghisla S.; "Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma."; Protein Expr. Purif. 52:89-95(2007).
[4]	BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1016/j.toxicon.2006.05.004; PubMed=16828829 [NCBI, ExPASy, EBI, Israel, Japan] Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.; "L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria."; Toxicon 48:227-237(2006).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-190 AND ASN-379. TISSUE=Venom; DOI=10.1093/emboj/19.16.4204; PubMed=10944103 [NCBI, ExPASy, EBI, Israel, Japan] Pawelek P.D., Cheah J., Coulombe R., Macheroux P., Ghisla S., Vrielink A.; "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site."; EMBO J. 19:4204-4215(2000).
[6]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF LAAO IN COMPLEX WITH THE SUBSTRATE L-PHE. TISSUE=Venom; DOI=10.1016/j.jmb.2006.09.032; PubMed=17046020 [NCBI, ExPASy, EBI, Israel, Japan] Moustafa I.M., Foster S., Lyubimov A.Y., Vrielink A.; "Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism."; J. Mol. Biol. 364:991-1002(2006).

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.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:   K_M=0.63 mM for L-Leu;
K_M=0.24 mM for L-Met;
K_M=0.08 mM for L-Trp;
pH dependence:   Optimum pH is 9.0;
Temperature dependence:   Thermostable;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
MISCELLANEOUS: This protein constitutes 30% of the venom.
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

AJ271725; CAB71136.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1F8R; X-ray; 2.00 A; A/B/C/D=19-516.	[ExPASy / RCSB / EBI]
1F8S; X-ray; 2.00 A; A/B/C/D/E/F/G/H=19-516.	[ExPASy / RCSB / EBI]
2IID; X-ray; 1.80 A; A/B/C/D=19-516.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1F8R; -.
1F8S; -.
2IID; -.

ModBase

P81382.

PTM databases

GlycoSuiteDB

P81382; -.

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.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

P81382.

Phylogenomic databases

HOVERGEN

P81382; -.

Other

ProtoNet

P81382.

UniRef

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

Keywords

3D-structure; Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`CHAIN`	`19 516`	`498`	`L-amino-acid oxidase.`	`PRO_0000001707`
`NP_BIND`	`43 44`	`2`	`FAD.`
`NP_BIND`	`63 71`	`9`	`FAD.`
`NP_BIND`	`89 90`	`2`	`FAD.`
`NP_BIND`	`464 469`	`6`	`FAD.`
`BINDING`	`89 89`		`FAD; via amide nitrogen.`
`BINDING`	`108 108`		`Substrate.`
`BINDING`	`279 279`		`FAD; via amide nitrogen and carbonyl oxygen.`
`BINDING`	`390 390`		`Substrate.`
`BINDING`	`475 475`		`FAD; via amide nitrogen.`
`BINDING`	`482 482`		`Substrate; via carbonyl oxygen.`
`CARBOHYD`	`190 190`		`N-linked (GlcNAc...).`
`CARBOHYD`	`379 379`		`N-linked (GlcNAc...).`
`DISULFID`	`28 191`
`DISULFID`	`349 430`
`CONFLICT`	`28 28`		`C -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`33 33`		`D -> N (in Ref. 2; AA sequence).`
`HELIX`	`26 29`	`4`
`HELIX`	`34 43`	`10`
`STRAND`	`53 57`	`5`
`HELIX`	`61 72`	`12`
`STRAND`	`76 80`	`5`
`STRAND`	`82 87`	`6`
`STRAND`	`92 95`	`4`
`TURN`	`96 99`	`4`
`STRAND`	`100 105`	`6`
`HELIX`	`114 122`	`9`
`STRAND`	`127 130`	`4`
`STRAND`	`137 141`	`5`
`STRAND`	`144 147`	`4`
`HELIX`	`148 153`	`6`
`HELIX`	`155 158`	`4`
`TURN`	`164 168`	`5`
`HELIX`	`171 178`	`8`
`HELIX`	`180 188`	`9`
`HELIX`	`191 197`	`7`
`STRAND`	`200 202`	`3`
`HELIX`	`203 209`	`7`
`HELIX`	`215 224`	`10`
`HELIX`	`228 230`	`3`
`HELIX`	`235 245`	`11`
`STRAND`	`251 254`	`4`
`HELIX`	`260 268`	`9`
`HELIX`	`269 272`	`4`
`STRAND`	`273 276`	`4`
`STRAND`	`278 284`	`7`
`STRAND`	`289 294`	`6`
`STRAND`	`296 298`	`3`
`STRAND`	`302 310`	`9`
`HELIX`	`314 317`	`4`
`STRAND`	`320 324`	`5`
`HELIX`	`328 336`	`9`
`STRAND`	`342 351`	`10`
`HELIX`	`353 357`	`5`
`STRAND`	`363 368`	`6`
`STRAND`	`372 374`	`3`
`STRAND`	`385 392`	`8`
`HELIX`	`393 397`	`5`
`TURN`	`398 401`	`4`
`HELIX`	`404 418`	`15`
`HELIX`	`423 429`	`7`
`STRAND`	`430 437`	`8`
`HELIX`	`438 440`	`3`
`TURN`	`442 444`	`3`
`STRAND`	`446 449`	`4`
`HELIX`	`455 464`	`10`
`STRAND`	`470 472`	`3`
`HELIX`	`475 477`	`3`
`STRAND`	`478 482`	`5`
`HELIX`	`484 503`	`20`

Sequence information

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

Molecular weight: 58221 Da [This is the MW of the unprocessed precursor]

CRC64: 5F9435718B3A3BDE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFDLRLNEF SQENDNAWYF IKNIRKKVGE VKKDPGLLKY PVKPSEAGKS AGQLYEESLG 

       190        200        210        220        230        240 
KVVEELKRTN CSYILNKYDT YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET 

       310        320        330        340        350        360 
PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT TKFWEDDGIH 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ ALDFKDCADI VFNDLSLIHQ 

       430        440        450        460        470        480 
LPKKDIQSFC YPSVIQKWSL DKYAMGGITT FTPYQFQHFS DPLTASQGRI YFAGEYTAQA 

       490        500        510 
HGWIDSTIKS GLRAARDVNL ASENPSGIHL SNDNEL

P81382 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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