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P81382

- OXLA_CALRH

UniProt

P81382 - OXLA_CALRH

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
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    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

    FAD.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891FAD2 Publications
    Binding sitei108 – 1081Substrate
    Binding sitei241 – 2411Substrate
    Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei390 – 3901Substrate
    Binding sitei475 – 4751FAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 622FAD2 Publications
    Nucleotide bindingi81 – 822FAD2 Publications
    Nucleotide bindingi105 – 1084FAD2 Publications
    Nucleotide bindingi482 – 4876FAD2 Publications
    Nucleotide bindingi482 – 4832Substrate

    GO - Molecular functioni

    1. L-amino-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cytolysis Source: UniProtKB-KW
    3. defense response to bacterium Source: UniProtKB-KW

    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

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 516498L-amino-acid oxidasePRO_0000001707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 1911 Publication
    Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
    Disulfide bondi349 ↔ 4301 Publication
    Glycosylationi379 – 3791N-linked (GlcNAc...)1 Publication

    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

    1
    516
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 294
    Helixi34 – 4310
    Beta strandi53 – 575
    Helixi61 – 7313
    Beta strandi76 – 805
    Beta strandi82 – 876
    Beta strandi92 – 954
    Turni96 – 994
    Beta strandi100 – 1056
    Helixi114 – 1229
    Beta strandi127 – 1304
    Beta strandi137 – 1415
    Beta strandi144 – 1474
    Helixi148 – 1536
    Helixi155 – 1584
    Helixi164 – 1663
    Helixi171 – 1788
    Helixi180 – 1889
    Helixi191 – 1988
    Beta strandi200 – 2023
    Helixi203 – 2097
    Helixi215 – 22410
    Helixi228 – 2303
    Helixi235 – 24511
    Beta strandi251 – 2544
    Helixi260 – 2689
    Helixi269 – 2724
    Beta strandi273 – 2764
    Beta strandi278 – 2847
    Beta strandi289 – 2946
    Beta strandi296 – 2983
    Beta strandi302 – 3109
    Helixi314 – 3174
    Beta strandi320 – 3245
    Helixi328 – 3369
    Beta strandi342 – 35110
    Helixi353 – 3575
    Beta strandi361 – 3688
    Beta strandi372 – 3743
    Beta strandi385 – 3928
    Helixi393 – 3975
    Turni398 – 4014
    Helixi404 – 41916
    Helixi423 – 4297
    Beta strandi430 – 4378
    Helixi438 – 4403
    Turni442 – 4443
    Beta strandi446 – 4494
    Helixi455 – 46410
    Beta strandi470 – 4723
    Helixi475 – 4773
    Beta strandi478 – 4825
    Helixi484 – 50320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 22-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81382.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P81382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN    50
    PKHVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW 100
    YANLGPMRLP EKHRIVREYI RKFDLRLNEF SQENDNAWYF IKNIRKKVGE 150
    VKKDPGLLKY PVKPSEAGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT 200
    YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR 250
    FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET 300
    PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT 350
    TKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ 400
    ALDFKDCADI VFNDLSLIHQ LPKKDIQSFC YPSVIQKWSL DKYAMGGITT 450
    FTPYQFQHFS DPLTASQGRI YFAGEYTAQA HGWIDSTIKS GLRAARDVNL 500
    ASENPSGIHL SNDNEL 516
    Length:516
    Mass (Da):58,221
    Last modified:January 23, 2002 - v2
    Checksum:i5F9435718B3A3BDE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281C → E AA sequence (PubMed:8080286)Curated
    Sequence conflicti33 – 331D → N AA sequence (PubMed:8080286)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271725 mRNA. Translation: CAB71136.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271725 mRNA. Translation: CAB71136.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F8R X-ray 2.00 A/B/C/D 19-516 [» ]
    1F8S X-ray 2.00 A/B/C/D/E/F/G/H 19-516 [» ]
    2IID X-ray 1.80 A/B/C/D 19-516 [» ]
    ProteinModelPortali P81382.
    SMRi P81382. Positions 22-504.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    UniCarbKBi P81382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005729.

    Enzyme and pathway databases

    SABIO-RK P81382.

    Miscellaneous databases

    EvolutionaryTracei P81382.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "L-amino-acid oxidase from Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzyme."
      Macheroux P., Seth O., Bollschweiler C., Schwarz M., Kurfuerst M., Au L.-C., Ghisla S.
      Eur. J. Biochem. 268:1679-1686(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-33.
      Tissue: Venom and Venom gland.
    2. "Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
      Ponnudurai G., Chung M.C.M., Tan N.-H.
      Arch. Biochem. Biophys. 313:373-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-38, SUBUNIT.
      Tissue: Venom.
    3. "Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma."
      Kommoju P.R., Macheroux P., Ghisla S.
      Protein Expr. Purif. 52:89-95(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPRESSION OF ACTIVE RECOMBINANT LAAO.
    4. "L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria."
      Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.
      Toxicon 48:227-237(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    5. "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site."
      Pawelek P.D., Cheah J., Coulombe R., Macheroux P., Ghisla S., Vrielink A.
      EMBO J. 19:4204-4215(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379.
      Tissue: Venom.
    6. "Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism."
      Moustafa I.M., Foster S., Lyubimov A.Y., Vrielink A.
      J. Mol. Biol. 364:991-1002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD AND SUBSTRATE L-PHE.
      Tissue: Venom.

    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: October 1, 2014
    This is version 90 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

    External Data

    Dasty 3