ID OXLA_NAJAT Reviewed; 507 AA. AC A8QL58; A0A2R4N4Q6; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 16-OCT-2019, sequence version 2. DT 03-MAY-2023, entry version 51. DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:17543361}; DE Short=LAO; DE Short=NA-LAAO {ECO:0000303|PubMed:18180850}; DE EC=1.4.3.2 {ECO:0000269|PubMed:18180850}; DE Flags: Precursor; Fragment; OS Naja atra (Chinese cobra). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja. OX NCBI_TaxID=8656; RN [1] {ECO:0000312|EMBL:AVX27607.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RA Chiang L.C., Mao Y.C.-C., Wu W.G.; RT "Isolation and characterization of L-amino acid oxidase from Naja atra RT snake venom."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000312|EMBL:ABN72546.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-449. RC TISSUE=Venom gland; RX PubMed=17543361; DOI=10.1016/j.toxicon.2007.04.013; RA Jin Y., Lee W.-H., Zeng L., Zhang Y.; RT "Molecular characterization of L-amino acid oxidase from king cobra RT venom."; RL Toxicon 50:479-489(2007). RN [3] RP PROTEIN SEQUENCE OF 20-29, FUNCTION IN PLATELET AGGREGATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND CATALYTIC RP ACTIVITY. RC TISSUE=Venom; RX PubMed=18180850; DOI=10.1111/j.1745-7270.2008.00372.x; RA Li R., Zhu S., Wu J., Wang W., Lu Q., Clemetson K.J.; RT "L-amino acid oxidase from Naja atra venom activates and binds to human RT platelets."; RL Acta Biochim. Biophys. Sin. 40:19-26(2008). RN [4] {ECO:0007744|PDB:5Z2G} RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH FAD, GLYCOSYLATION RP AT ASN-191; ASN-213 AND ASN-378, DISULFIDE BONDS, COFACTOR, AND SUBUNIT. RA Kumar J.V., Chien K.Y., Lin C.C., Chiang L.C., Lin T.H., Wu W.G.; RT "Crystal structure of L-amino acid oxidase from naja atra (Taiwan Cobra)."; RL Submitted (JAN-2018) to the PDB data bank. 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:18180850). Shows activity on L-Leu (PubMed:18180850). CC Exhibits diverse biological activities, such as hemorrhage, hemolysis, CC edema, apoptosis of vascular endothelial cells or tumor cell lines, CC antibacterial and antiparasitic activities (By similarity). This CC protein induces platelet aggregation by both hydrogen peroxide CC production and binding to platelet membrane proteins (that would CC enhance the sensitivity of platelets to hydrogen peroxide). Effects of CC snake L-amino oxidases on platelets are controversial, since they CC either induce aggregation or inhibit agonist-induced aggregation. These CC different effects are probably due to different experimental CC conditions. {ECO:0000250|UniProtKB:P0CC17, CC ECO:0000269|PubMed:18180850}. 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:18180850}; 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:18180850}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.4}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=38.4 umol/min/mg enzyme {ECO:0000269|PubMed:18180850}; CC -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000269|Ref.4}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18180850}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:18180850}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF080839; ABN72546.1; -; mRNA. DR EMBL; MH023324; AVX27607.1; -; mRNA. DR PDB; 5Z2G; X-ray; 2.68 A; A/B=1-507. DR PDBsum; 5Z2G; -. DR AlphaFoldDB; A8QL58; -. DR SMR; A8QL58; -. DR BRENDA; 1.4.3.2; 3558. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC. 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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR Gene3D; 3.90.660.10; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR001613; Flavin_amine_oxidase. DR PANTHER; PTHR10742:SF235; AMINE OXIDASE; 1. DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Apoptosis; Cytolysis; KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein; KW Hemolysis; Hemostasis impairing toxin; Oxidoreductase; KW Platelet aggregation activating toxin; Secreted; Signal; Toxin. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:18180850" FT CHAIN 20..>507 FT /note="L-amino-acid oxidase" FT /id="PRO_0000412603" FT BINDING 62..63 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382, FT ECO:0007744|PDB:5Z2G" FT BINDING 82..83 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382, FT ECO:0007744|PDB:5Z2G" FT BINDING 90 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5Z2G" FT BINDING 106..109 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382, FT ECO:0007744|PDB:5Z2G" FT BINDING 109 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5Z2G" FT BINDING 389 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 473 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5Z2G" FT BINDING 480..485 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382, FT ECO:0007744|PDB:5Z2G" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007744|PDB:5Z2G" FT CARBOHYD 213 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007744|PDB:5Z2G" FT CARBOHYD 378 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007744|PDB:5Z2G" FT DISULFID 29..192 FT /evidence="ECO:0007744|PDB:5Z2G" FT DISULFID 348..429 FT /evidence="ECO:0007744|PDB:5Z2G" FT CONFLICT 28..38 FT /note="KCFQEADYEDF -> ECFQQNDYEEI (in Ref. 2; ABN72546)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="E -> K (in Ref. 2; ABN72546)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="S -> P (in Ref. 2; ABN72546)" FT /evidence="ECO:0000305" FT NON_TER 507 FT /evidence="ECO:0000303|Ref.1" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 35..44 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 54..58 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 62..73 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:5Z2G" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 115..123 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 149..154 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 156..159 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 172..178 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 192..199 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 204..210 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 216..225 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 236..246 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 261..269 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 270..273 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 290..309 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 313..318 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 327..335 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 341..350 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 352..356 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 360..367 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 384..391 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 392..398 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 403..417 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 422..428 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 429..435 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:5Z2G" FT TURN 440..442 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 443..447 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 453..462 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 468..470 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:5Z2G" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:5Z2G" FT HELIX 482..499 FT /evidence="ECO:0007829|PDB:5Z2G" SQ SEQUENCE 507 AA; 57963 MW; 4A67EDCDF9502A22 CRC64; MNVLFIFSLL FLAALESCAD DRRSPLEKCF QEADYEDFLE IARNGLKETS NPKHVVVVGA GMAGLSAAYV LAGAGHKVTL LEASERVGGR VITYHNDREG WYVNMGPMRL PERHRIVREY IRKFGLKLNE FFQENENAWY YINNIRKRVW EVKKDPSLLK YPVKPSEEGK SASQLYQESL RKVIEELKRT NCSYILNKYD SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYHLSFMESL KSDALFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNARV IKIQYDAEKV RVTYQTPAKT FVTADYVIVC STSRAARRIY FEPPLPPKKA HALRSIHYRS ATKIFLTCSK KFWEADGIHG GKSTTDLPSR FIHYPNHNFT SGIGVIMAYV LADDSDFFQA LDTKTCADIV INDLSLIHDL PKREIQALCY PSIKKWNLDK YTMGSITSFT PYQFQDYFES AAAPVGRIHF AGEYTGRFHG WIDSTIMTGL RAARDVNRAS QKPSKIR //