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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Gloydius halys (Chinese water mocassin) (Agkistrodon halys)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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, 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). This protein induces apoptosis of cultured HeLa cells.By similarity1 Publication

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89FAD2 Publications1
Binding sitei108Substrate1
Binding sitei241Substrate1
Binding sitei279FAD; via amide nitrogen and carbonyl oxygen2 Publications1
Binding sitei390Substrate1
Binding sitei475FAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi61 – 62FAD2 Publications2
Nucleotide bindingi81 – 82FAD2 Publications2
Nucleotide bindingi105 – 108FAD2 Publications4
Nucleotide bindingi482 – 487FAD2 Publications6
Nucleotide bindingi482 – 483Substrate2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemorrhagic toxin, Hemostasis impairing toxin, Oxidoreductase, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
AHP-LAAO
Short name:
LAAO
Short name:
LAO
OrganismiGloydius halys (Chinese water mocassin) (Agkistrodon halys)
Taxonomic identifieri8714 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000027356319 – 504L-amino-acid oxidaseAdd BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 191
Glycosylationi190N-linked (GlcNAc...)2 Publications1
Disulfide bondi349 ↔ 430
Glycosylationi379N-linked (GlcNAc...)2 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.2 Publications

Structurei

Secondary structure

1504
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 29Combined sources4
Helixi34 – 43Combined sources10
Beta strandi53 – 57Combined sources5
Helixi61 – 72Combined sources12
Beta strandi76 – 80Combined sources5
Beta strandi82 – 86Combined sources5
Beta strandi92 – 95Combined sources4
Turni96 – 99Combined sources4
Beta strandi100 – 105Combined sources6
Beta strandi109 – 112Combined sources4
Helixi114 – 122Combined sources9
Beta strandi127 – 129Combined sources3
Beta strandi137 – 141Combined sources5
Beta strandi144 – 147Combined sources4
Helixi148 – 153Combined sources6
Helixi155 – 158Combined sources4
Helixi164 – 166Combined sources3
Helixi171 – 178Combined sources8
Helixi180 – 188Combined sources9
Helixi191 – 197Combined sources7
Helixi198 – 200Combined sources3
Helixi203 – 209Combined sources7
Helixi215 – 224Combined sources10
Helixi228 – 230Combined sources3
Beta strandi231 – 234Combined sources4
Helixi235 – 245Combined sources11
Beta strandi251 – 254Combined sources4
Helixi260 – 268Combined sources9
Helixi269 – 272Combined sources4
Beta strandi273 – 276Combined sources4
Beta strandi278 – 285Combined sources8
Beta strandi288 – 294Combined sources7
Beta strandi296 – 298Combined sources3
Beta strandi300 – 310Combined sources11
Helixi314 – 318Combined sources5
Beta strandi320 – 324Combined sources5
Helixi328 – 336Combined sources9
Beta strandi342 – 351Combined sources10
Helixi353 – 357Combined sources5
Beta strandi363 – 368Combined sources6
Beta strandi372 – 374Combined sources3
Beta strandi385 – 392Combined sources8
Helixi393 – 397Combined sources5
Turni398 – 401Combined sources4
Helixi404 – 419Combined sources16
Helixi423 – 429Combined sources7
Beta strandi430 – 437Combined sources8
Helixi438 – 440Combined sources3
Turni442 – 444Combined sources3
Beta strandi446 – 449Combined sources4
Helixi455 – 464Combined sources10
Beta strandi470 – 472Combined sources3
Helixi475 – 477Combined sources3
Beta strandi478 – 480Combined sources3
Helixi484 – 503Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1REOX-ray2.31A19-504[»]
1TDKX-ray2.70A19-504[»]
1TDNX-ray2.70A19-504[»]
1TDOX-ray3.00A19-504[»]
ProteinModelPortaliQ6STF1.
SMRiQ6STF1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6STF1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6STF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAN DRNPLEECFR ETDYEEFLEI ARNGLKATSN
60 70 80 90 100
PKHVVVVGAG MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEDW
110 120 130 140 150
YANLGPMRLP EKHRIVREYI RKFGLQLNEF SQENDNAWYF IKNIRKRVGE
160 170 180 190 200
VKKDPGVLKY PVKPSEEGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT
210 220 230 240 250
YSTKEYLLKE GNLSPGAVDM IGDLMNEDSG YYVSFPESLR HDDIFAYEKR
260 270 280 290 300
FDEIVGGMDK LPTSMYRAIE EKVHLNAQVI KIQKNAEKVT VVYQTPAKEM
310 320 330 340 350
ASVTADYVIV CTTSRATRRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT
360 370 380 390 400
KKFWEDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDFKDCADI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT
460 470 480 490 500
FTPYQFQHFS ESLTASVDRI YFAGEHTAEA HGWIDSTIKS GLRAARDVNR

ASEQ
Length:504
Mass (Da):57,125
Last modified:July 5, 2004 - v1
Checksum:iAEB034155184F0A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY450403 mRNA. Translation: AAR20248.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY450403 mRNA. Translation: AAR20248.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1REOX-ray2.31A19-504[»]
1TDKX-ray2.70A19-504[»]
1TDNX-ray2.70A19-504[»]
1TDOX-ray3.00A19-504[»]
ProteinModelPortaliQ6STF1.
SMRiQ6STF1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005729.

Miscellaneous databases

EvolutionaryTraceiQ6STF1.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiOXLA_GLOHA
AccessioniPrimary (citable) accession number: Q6STF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.