OXLA1_BOTJR
ID OXLA1_BOTJR Reviewed; 497 AA.
AC Q6TGQ9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=L-amino-acid oxidase BjussuLAAO-I {ECO:0000303|PubMed:17292326};
DE Short=BjsuLAAO {ECO:0000303|PubMed:22490662};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:22490662};
DE Flags: Precursor; Fragment;
OS Bothrops jararacussu (Jararacussu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8726;
RN [1] {ECO:0000312|EMBL:AAR31182.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=17292326; DOI=10.1016/j.bbrc.2006.12.217;
RA Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O.,
RA Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V.,
RA Soares A.M.;
RT "Molecular approaches for structural characterization of Bothrops L-amino
RT acid oxidases with antiprotozoal activity: cDNA cloning, comparative
RT sequence analysis, and molecular modeling.";
RL Biochem. Biophys. Res. Commun. 355:302-306(2007).
RN [2] {ECO:0000312|PDB:4E0V}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 18-496 IN COMPLEX WITH FAD,
RP DISULFIDE BOND, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=22490662; DOI=10.1016/j.bbrc.2012.03.129;
RA Ullah A., Souza T.A., Abrego J.R., Betzel C., Murakami M.T., Arni R.K.;
RT "Structural insights into selectivity and cofactor binding in snake venom
RT L-amino acid oxidases.";
RL Biochem. Biophys. Res. Commun. 421:124-128(2012).
CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC peroxide that may contribute to the diverse toxic effects of this
CC enzyme (PubMed:22490662). Shows high specificity for L-Met, L-Leu, L-
CC Phe, L-Tyr, L-Ile, L-Trp, a moderate activity on L-Cys and low activity
CC on L-Val, L-Lys, L-Arg, L-His, L-Gln, L-Thr and L-Ser
CC (PubMed:22490662). Exhibits diverse biological activities, such as
CC hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells
CC or tumor cell lines, and antibacterial, as well as regulation of
CC platelet aggregation (By similarity). Effects of snake L-amino oxidases
CC on platelets are controversial, since they either induce aggregation or
CC inhibit agonist-induced aggregation (By similarity). These different
CC effects are probably due to different experimental conditions (By
CC similarity). In vitro, shows parasiticidal activities against both
CC trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen
CC peroxide production.(PubMed:17292326). {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:17292326, ECO:0000269|PubMed:22490662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2;
CC Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844;
CC Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2
CC + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146,
CC ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:22490662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteine + O2 = 2-oxo-3-sulfanylpropanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57678; Evidence={ECO:0000269|PubMed:22490662};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:22490662};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:22490662}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22490662}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22490662}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY398691; AAR31182.1; -; mRNA.
DR PDB; 4E0V; X-ray; 3.10 A; A/B=18-496.
DR PDBsum; 4E0V; -.
DR AlphaFoldDB; Q6TGQ9; -.
DR SMR; Q6TGQ9; -.
DR BRENDA; 1.4.3.2; 6809.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Apoptosis; Cytolysis;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW Hemostasis impairing toxin; Nucleotide-binding; Oxidoreductase; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..13
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CHAIN 14..>497
FT /note="L-amino-acid oxidase BjussuLAAO-I"
FT /id="PRO_0000273564"
FT BINDING 56..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT BINDING 76..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT BINDING 76..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT BINDING 100..103
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 470
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT BINDING 477..482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 477..478
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 478..482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4E0V"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..186
FT /evidence="ECO:0000269|PubMed:22490662,
FT ECO:0007744|PDB:4E0V"
FT DISULFID 344..425
FT /evidence="ECO:0000269|PubMed:22490662,
FT ECO:0007744|PDB:4E0V"
FT NON_TER 497
FT /evidence="ECO:0000303|PubMed:17292326"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 179..184
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 223..227
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 323..331
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 399..413
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 418..423
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:4E0V"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:4E0V"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:4E0V"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:4E0V"
SQ SEQUENCE 497 AA; 56289 MW; 51AFCB28038399A1 CRC64;
MNVFFMFSKP GKLADDRNPL EECFRETDYE EFLEIAKNGL STTSNPKRVV IVGAGMSGLS
AAYVLANAGH QVTVLEASER AGGQVKTYRN EKEGWYANLG PMRLPEKHRI VREYIRKFGL
QLNEFSQENE NAWYFIKNIR KRVGEVNKDP GVLDYPVKPS EVGKSAGQLY EESLQKAVEE
LRRTNCSYML NKYDTYSTKE YLLKEGNLSP GAVDMIGDLL NEDSGYYVSF IESLKHDDIF
AYEKRFDEIV GGMDKLPTSM YQAIQEKVHL NARVIKIQQD VKEVTVTYQT SEKETLSVTA
DYVIVCTTSR AARRIKFEPP LPPKKAHALR SVHYRSGTKI FLTCTKKFWE DDGIHGGKST
TDLPSRFIYY PNHNFPNGVG VIIAYGIGDD ANYFEALDFE DCGDIVINDL SLIHQLPKEE
IQAICRPSMI QRWSLDKYAM GGITTFTPYQ FQHFSEALTA PVDRIYFAGE YTAQAHGWIA
STIKSGPEGL DVNRASE
