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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
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, 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).By similarity

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.63 mM for L-Leu1 Publication
  2. KM=0.24 mM for L-Met1 Publication
  3. KM=0.05 mM for L-Phe1 Publication
  4. KM=0.08 mM for L-Trp1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Temperature dependencei

    Thermostable.1 Publication

    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, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    SABIO-RKP81382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
    Taxonomic identifieri8717 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 182 PublicationsAdd BLAST18
    ChainiPRO_000000170719 – 516L-amino-acid oxidaseAdd BLAST498

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi28 ↔ 1911 Publication
    Glycosylationi190N-linked (GlcNAc...)1 Publication1
    Disulfide bondi349 ↔ 4301 Publication
    Glycosylationi379N-linked (GlcNAc...)1 Publication1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    PTM databases

    UniCarbKBiP81382.

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.3 Publications

    Structurei

    Secondary structure

    1516
    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 – 73Combined sources13
    Beta strandi76 – 80Combined sources5
    Beta strandi82 – 87Combined sources6
    Beta strandi92 – 95Combined sources4
    Turni96 – 99Combined sources4
    Beta strandi100 – 105Combined sources6
    Helixi114 – 122Combined sources9
    Beta strandi127 – 130Combined sources4
    Beta strandi137 – 141Combined sources5
    Beta strandi144 – 147Combined sources4
    Helixi148 – 153Combined sources6
    Helixi155 – 158Combined sources4
    Helixi164 – 166Combined sources3
    Helixi171 – 178Combined sources8
    Helixi180 – 188Combined sources9
    Helixi191 – 198Combined sources8
    Beta strandi200 – 202Combined sources3
    Helixi203 – 209Combined sources7
    Helixi215 – 224Combined sources10
    Helixi228 – 230Combined sources3
    Helixi235 – 245Combined sources11
    Beta strandi251 – 254Combined sources4
    Helixi260 – 268Combined sources9
    Helixi269 – 272Combined sources4
    Beta strandi273 – 276Combined sources4
    Beta strandi278 – 284Combined sources7
    Beta strandi289 – 294Combined sources6
    Beta strandi296 – 298Combined sources3
    Beta strandi302 – 310Combined sources9
    Helixi314 – 317Combined sources4
    Beta strandi320 – 324Combined sources5
    Helixi328 – 336Combined sources9
    Beta strandi342 – 351Combined sources10
    Helixi353 – 357Combined sources5
    Beta strandi361 – 368Combined sources8
    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 – 482Combined sources5
    Helixi484 – 503Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F8RX-ray2.00A/B/C/D19-516[»]
    1F8SX-ray2.00A/B/C/D/E/F/G/H19-516[»]
    2IIDX-ray1.80A/B/C/D19-516[»]
    ProteinModelPortaliP81382.
    SMRiP81382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81382.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_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.

    P81382-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN
    60 70 80 90 100
    PKHVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW
    110 120 130 140 150
    YANLGPMRLP EKHRIVREYI RKFDLRLNEF SQENDNAWYF IKNIRKKVGE
    160 170 180 190 200
    VKKDPGLLKY PVKPSEAGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT
    210 220 230 240 250
    YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR
    260 270 280 290 300
    FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET
    310 320 330 340 350
    PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT
    360 370 380 390 400
    TKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ
    410 420 430 440 450
    ALDFKDCADI VFNDLSLIHQ LPKKDIQSFC YPSVIQKWSL DKYAMGGITT
    460 470 480 490 500
    FTPYQFQHFS DPLTASQGRI YFAGEYTAQA HGWIDSTIKS GLRAARDVNL
    510
    ASENPSGIHL SNDNEL
    Length:516
    Mass (Da):58,221
    Last modified:January 23, 2002 - v2
    Checksum:i5F9435718B3A3BDE
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti28C → E AA sequence (PubMed:8080286).Curated1
    Sequence conflicti33D → N AA sequence (PubMed:8080286).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271725 mRNA. Translation: CAB71136.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271725 mRNA. Translation: CAB71136.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F8RX-ray2.00A/B/C/D19-516[»]
    1F8SX-ray2.00A/B/C/D/E/F/G/H19-516[»]
    2IIDX-ray1.80A/B/C/D19-516[»]
    ProteinModelPortaliP81382.
    SMRiP81382.
    ModBaseiSearch...
    MobiDBiSearch...

    PTM databases

    UniCarbKBiP81382.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOVERGENiHBG005729.

    Enzyme and pathway databases

    SABIO-RKP81382.

    Miscellaneous databases

    EvolutionaryTraceiP81382.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiOXLA_CALRH
    AccessioniPrimary (citable) accession number: P81382
    Secondary accession number(s): Q9I849
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2002
    Last modified: November 2, 2016
    This is version 98 of the entry and version 2 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.