X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 19-504, PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379, FUNCTION, AND MASS SPECTROMETRY.
TISSUE=Venom;
DOI=10.1107/S0907444904000046; PubMed=15103157 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Teng M., Niu L., Wang Y., Wang Y., Liu Q., Huang Q., Hao Q., Dong Y., Liu P.;
"Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom.";
Acta Crystallogr. D 60:974-977(2004).

Comments

FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Inhibits platelet aggregation and has an ability to induce hemorrhage. Has an antibacterial activity (By similarity). Induces apoptosis of cultured HeLa cells.
CATALYTIC ACTIVITY: An L-amino acid + H₂O + O₂ = a 2-oxo acid + NH₃ + H₂O₂.
COFACTOR: FAD.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
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

AY450403; AAR20248.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1REO; X-ray; 2.31 A; A=19-504.

[ExPASy / RCSB / EBI]

PDBsum

1REO; -.

ModBase

Q6STF1.

Ontologies

GO:0001716;	Molecular function: L-amino-acid oxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR002937; Amino_oxidase.
Graphical view of domain structure.

Pfam

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

PRINTS

PR00419; ADXRDTASE.

BLOCKS

Q6STF1.

Phylogenomic databases

HOVERGEN

Q6STF1; -.

Other

ProtoNet

Q6STF1.

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`	`19 504`	`486`	`L-amino-acid oxidase.`	`PRO_0000273563`
`NP_BIND`	`107 108`	`2`	`FAD.`
`NP_BIND`	`475 487`	`13`	`FAD.`
`BINDING`	`62 62`		`FAD.`
`BINDING`	`81 81`		`FAD.`
`BINDING`	`89 89`		`FAD.`
`BINDING`	`108 108`		`Substrate.`
`BINDING`	`241 241`		`Substrate.`
`BINDING`	`279 279`		`FAD; via amide nitrogen and carbonyl oxygen.`
`BINDING`	`390 390`		`Substrate.`
`CARBOHYD`	`190 190`		`N-linked (GlcNAc...).`
`CARBOHYD`	`379 379`		`N-linked (GlcNAc...).`
`DISULFID`	`28 191`
`DISULFID`	`349 430`
`HELIX`	`26 29`	`4`
`HELIX`	`34 43`	`10`
`STRAND`	`53 57`	`5`
`HELIX`	`61 72`	`12`
`STRAND`	`76 80`	`5`
`STRAND`	`82 86`	`5`
`STRAND`	`92 95`	`4`
`TURN`	`96 99`	`4`
`STRAND`	`100 105`	`6`
`HELIX`	`114 122`	`9`
`STRAND`	`127 129`	`3`
`STRAND`	`137 141`	`5`
`STRAND`	`144 147`	`4`
`HELIX`	`148 153`	`6`
`HELIX`	`155 158`	`4`
`HELIX`	`164 166`	`3`
`HELIX`	`171 178`	`8`
`HELIX`	`180 188`	`9`
`HELIX`	`191 197`	`7`
`HELIX`	`198 200`	`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`	`278 285`	`8`
`STRAND`	`288 294`	`7`
`STRAND`	`296 298`	`3`
`STRAND`	`300 310`	`11`
`HELIX`	`314 318`	`5`
`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`	`404 419`	`16`
`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`	`478 480`	`3`
`HELIX`	`484 503`	`20`

Sequence information

Length: 504 AA [This is the length of the unprocessed precursor]

Molecular weight: 57125 Da [This is the MW of the unprocessed precursor]

CRC64: AEB034155184F0A7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAN DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVVVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEDW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFGLQLNEF SQENDNAWYF IKNIRKRVGE VKKDPGVLKY PVKPSEEGKS AGQLYEESLG 

       190        200        210        220        230        240 
KVVEELKRTN CSYILNKYDT YSTKEYLLKE GNLSPGAVDM IGDLMNEDSG YYVSFPESLR 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVGGMDK LPTSMYRAIE EKVHLNAQVI KIQKNAEKVT VVYQTPAKEM 

       310        320        330        340        350        360 
ASVTADYVIV CTTSRATRRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDEGIH 

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

       430        440        450        460        470        480 
LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS ESLTASVDRI YFAGEHTAEA 

       490        500 
HGWIDSTIKS GLRAARDVNR ASEQ

Q6STF1 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